3v65: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
m Protected "3v65" [edit=sysop:move=sysop]
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 3v65 is ON HOLD
==Crystal structure of agrin and LRP4 complex==
<StructureSection load='3v65' size='340' side='right'caption='[[3v65]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3v65]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V65 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v64|3v64]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Agrn, Agrin ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Lrp4, Megf7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v65 OCA], [https://pdbe.org/3v65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v65 RCSB], [https://www.ebi.ac.uk/pdbsum/3v65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v65 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/AGRIN_RAT AGRIN_RAT]] Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.<ref>PMID:8398142</ref> <ref>PMID:8653787</ref> <ref>PMID:8693000</ref> <ref>PMID:18775496</ref> <ref>PMID:19524020</ref> <ref>PMID:20471381</ref> <ref>PMID:20566625</ref> <ref>PMID:20505824</ref>  Isoform 1, isoform 4, isoform 5 and isoform 6: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.<ref>PMID:8398142</ref> <ref>PMID:8653787</ref> <ref>PMID:8693000</ref> <ref>PMID:18775496</ref> <ref>PMID:19524020</ref> <ref>PMID:20471381</ref> <ref>PMID:20566625</ref> <ref>PMID:20505824</ref>  Agrin N-terminal 110 kDa subunit: is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity).<ref>PMID:8398142</ref> <ref>PMID:8653787</ref> <ref>PMID:8693000</ref> <ref>PMID:18775496</ref> <ref>PMID:19524020</ref> <ref>PMID:20471381</ref> <ref>PMID:20566625</ref> <ref>PMID:20505824</ref>  Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.<ref>PMID:8398142</ref> <ref>PMID:8653787</ref> <ref>PMID:8693000</ref> <ref>PMID:18775496</ref> <ref>PMID:19524020</ref> <ref>PMID:20471381</ref> <ref>PMID:20566625</ref> <ref>PMID:20505824</ref>  [[https://www.uniprot.org/uniprot/LRP4_RAT LRP4_RAT]] Mediates SOST-dependent inhibition of bone formation (By similarity). Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling (By similarity). Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Synapses are the fundamental units of neural circuits that enable complex behaviors. The neuromuscular junction (NMJ), a synapse formed between a motoneuron and a muscle fiber, has contributed greatly to understanding of the general principles of synaptogenesis as well as of neuromuscular disorders. NMJ formation requires neural agrin, a motoneuron-derived protein, which interacts with LRP4 (low-density lipoprotein receptor-related protein 4) to activate the receptor tyrosine kinase MuSK (muscle-specific kinase). However, little is known of how signals are transduced from agrin to MuSK. Here, we present the first crystal structure of an agrin-LRP4 complex, consisting of two agrin-LRP4 heterodimers. Formation of the initial binary complex requires the z8 loop that is specifically present in neuronal, but not muscle, agrin and that promotes the synergistic formation of the tetramer through two additional interfaces. We show that the tetrameric complex is essential for neuronal agrin-induced acetylcholine receptor (AChR) clustering. Collectively, these results provide new insight into the agrin-LRP4-MuSK signaling cascade and NMJ formation and represent a novel mechanism for activation of receptor tyrosine kinases.


Authors: Zong, Y., Jin, R.
Structural basis of agrin-LRP4-MuSK signaling.,Zong Y, Zhang B, Gu S, Lee K, Zhou J, Yao G, Figueiredo D, Perry K, Mei L, Jin R Genes Dev. 2012 Feb 1;26(3):247-58. doi: 10.1101/gad.180885.111. PMID:22302937<ref>PMID:22302937</ref>


Description: Crystal structure of agrin and LRP4 complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3v65" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Agrin 3D structures|Agrin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Jin, R]]
[[Category: Zong, Y]]
[[Category: Beta-propeller]]
[[Category: Laminin-g]]
[[Category: Protein binding]]

Latest revision as of 11:34, 20 July 2022

Crystal structure of agrin and LRP4 complexCrystal structure of agrin and LRP4 complex

Structural highlights

3v65 is a 4 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:Agrn, Agrin (Buffalo rat), Lrp4, Megf7 (Buffalo rat)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AGRIN_RAT] Isoform 1: heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homestasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.[1] [2] [3] [4] [5] [6] [7] [8] Isoform 1, isoform 4, isoform 5 and isoform 6: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.[9] [10] [11] [12] [13] [14] [15] [16] Agrin N-terminal 110 kDa subunit: is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity).[17] [18] [19] [20] [21] [22] [23] [24] Agrin C-terminal 22 kDa fragment: this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.[25] [26] [27] [28] [29] [30] [31] [32] [LRP4_RAT] Mediates SOST-dependent inhibition of bone formation (By similarity). Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling (By similarity). Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes.

Publication Abstract from PubMed

Synapses are the fundamental units of neural circuits that enable complex behaviors. The neuromuscular junction (NMJ), a synapse formed between a motoneuron and a muscle fiber, has contributed greatly to understanding of the general principles of synaptogenesis as well as of neuromuscular disorders. NMJ formation requires neural agrin, a motoneuron-derived protein, which interacts with LRP4 (low-density lipoprotein receptor-related protein 4) to activate the receptor tyrosine kinase MuSK (muscle-specific kinase). However, little is known of how signals are transduced from agrin to MuSK. Here, we present the first crystal structure of an agrin-LRP4 complex, consisting of two agrin-LRP4 heterodimers. Formation of the initial binary complex requires the z8 loop that is specifically present in neuronal, but not muscle, agrin and that promotes the synergistic formation of the tetramer through two additional interfaces. We show that the tetrameric complex is essential for neuronal agrin-induced acetylcholine receptor (AChR) clustering. Collectively, these results provide new insight into the agrin-LRP4-MuSK signaling cascade and NMJ formation and represent a novel mechanism for activation of receptor tyrosine kinases.

Structural basis of agrin-LRP4-MuSK signaling.,Zong Y, Zhang B, Gu S, Lee K, Zhou J, Yao G, Figueiredo D, Perry K, Mei L, Jin R Genes Dev. 2012 Feb 1;26(3):247-58. doi: 10.1101/gad.180885.111. PMID:22302937[33]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Ferns MJ, Campanelli JT, Hoch W, Scheller RH, Hall Z. The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron. 1993 Sep;11(3):491-502. PMID:8398142
  2. ↑ Glass DJ, Bowen DC, Stitt TN, Radziejewski C, Bruno J, Ryan TE, Gies DR, Shah S, Mattsson K, Burden SJ, DiStefano PS, Valenzuela DM, DeChiara TM, Yancopoulos GD. Agrin acts via a MuSK receptor complex. Cell. 1996 May 17;85(4):513-23. PMID:8653787
  3. ↑ O'Toole JJ, Deyst KA, Bowe MA, Nastuk MA, McKechnie BA, Fallon JR. Alternative splicing of agrin regulates its binding to heparin alpha-dystroglycan, and the cell surface. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7369-74. PMID:8693000
  4. ↑ Kim ML, Chandrasekharan K, Glass M, Shi S, Stahl MC, Kaspar B, Stanley P, Martin PT. O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors. Mol Cell Neurosci. 2008 Nov;39(3):452-64. doi: 10.1016/j.mcn.2008.07.026. Epub, 2008 Aug 15. PMID:18775496 doi:http://dx.doi.org/10.1016/j.mcn.2008.07.026
  5. ↑ McCroskery S, Bailey A, Lin L, Daniels MP. Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures. Neuroscience. 2009 Sep 29;163(1):168-79. doi: 10.1016/j.neuroscience.2009.06.012., Epub 2009 Jun 10. PMID:19524020 doi:http://dx.doi.org/10.1016/j.neuroscience.2009.06.012
  6. ↑ Lin L, McCroskery S, Ross JM, Chak Y, Neuhuber B, Daniels MP. Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases. Exp Cell Res. 2010 Aug 15;316(14):2260-77. doi: 10.1016/j.yexcr.2010.05.006. Epub, 2010 May 13. PMID:20471381 doi:http://dx.doi.org/10.1016/j.yexcr.2010.05.006
  7. ↑ Tseng CN, Zhang L, Wu SL, Wang WF, Wang ZZ, Cascio M. Asparagine of z8 insert is critical for the affinity, conformation, and acetylcholine receptor-clustering activity of neural agrin. J Biol Chem. 2010 Sep 3;285(36):27641-51. doi: 10.1074/jbc.M110.130625. Epub 2010, Jun 21. PMID:20566625 doi:http://dx.doi.org/10.1074/jbc.M110.130625
  8. ↑ Banyai L, Sonderegger P, Patthy L. Agrin binds BMP2, BMP4 and TGFbeta1. PLoS One. 2010 May 21;5(5):e10758. doi: 10.1371/journal.pone.0010758. PMID:20505824 doi:http://dx.doi.org/10.1371/journal.pone.0010758
  9. ↑ Ferns MJ, Campanelli JT, Hoch W, Scheller RH, Hall Z. The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron. 1993 Sep;11(3):491-502. PMID:8398142
  10. ↑ Glass DJ, Bowen DC, Stitt TN, Radziejewski C, Bruno J, Ryan TE, Gies DR, Shah S, Mattsson K, Burden SJ, DiStefano PS, Valenzuela DM, DeChiara TM, Yancopoulos GD. Agrin acts via a MuSK receptor complex. Cell. 1996 May 17;85(4):513-23. PMID:8653787
  11. ↑ O'Toole JJ, Deyst KA, Bowe MA, Nastuk MA, McKechnie BA, Fallon JR. Alternative splicing of agrin regulates its binding to heparin alpha-dystroglycan, and the cell surface. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7369-74. PMID:8693000
  12. ↑ Kim ML, Chandrasekharan K, Glass M, Shi S, Stahl MC, Kaspar B, Stanley P, Martin PT. O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors. Mol Cell Neurosci. 2008 Nov;39(3):452-64. doi: 10.1016/j.mcn.2008.07.026. Epub, 2008 Aug 15. PMID:18775496 doi:http://dx.doi.org/10.1016/j.mcn.2008.07.026
  13. ↑ McCroskery S, Bailey A, Lin L, Daniels MP. Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures. Neuroscience. 2009 Sep 29;163(1):168-79. doi: 10.1016/j.neuroscience.2009.06.012., Epub 2009 Jun 10. PMID:19524020 doi:http://dx.doi.org/10.1016/j.neuroscience.2009.06.012
  14. ↑ Lin L, McCroskery S, Ross JM, Chak Y, Neuhuber B, Daniels MP. Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases. Exp Cell Res. 2010 Aug 15;316(14):2260-77. doi: 10.1016/j.yexcr.2010.05.006. Epub, 2010 May 13. PMID:20471381 doi:http://dx.doi.org/10.1016/j.yexcr.2010.05.006
  15. ↑ Tseng CN, Zhang L, Wu SL, Wang WF, Wang ZZ, Cascio M. Asparagine of z8 insert is critical for the affinity, conformation, and acetylcholine receptor-clustering activity of neural agrin. J Biol Chem. 2010 Sep 3;285(36):27641-51. doi: 10.1074/jbc.M110.130625. Epub 2010, Jun 21. PMID:20566625 doi:http://dx.doi.org/10.1074/jbc.M110.130625
  16. ↑ Banyai L, Sonderegger P, Patthy L. Agrin binds BMP2, BMP4 and TGFbeta1. PLoS One. 2010 May 21;5(5):e10758. doi: 10.1371/journal.pone.0010758. PMID:20505824 doi:http://dx.doi.org/10.1371/journal.pone.0010758
  17. ↑ Ferns MJ, Campanelli JT, Hoch W, Scheller RH, Hall Z. The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron. 1993 Sep;11(3):491-502. PMID:8398142
  18. ↑ Glass DJ, Bowen DC, Stitt TN, Radziejewski C, Bruno J, Ryan TE, Gies DR, Shah S, Mattsson K, Burden SJ, DiStefano PS, Valenzuela DM, DeChiara TM, Yancopoulos GD. Agrin acts via a MuSK receptor complex. Cell. 1996 May 17;85(4):513-23. PMID:8653787
  19. ↑ O'Toole JJ, Deyst KA, Bowe MA, Nastuk MA, McKechnie BA, Fallon JR. Alternative splicing of agrin regulates its binding to heparin alpha-dystroglycan, and the cell surface. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7369-74. PMID:8693000
  20. ↑ Kim ML, Chandrasekharan K, Glass M, Shi S, Stahl MC, Kaspar B, Stanley P, Martin PT. O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors. Mol Cell Neurosci. 2008 Nov;39(3):452-64. doi: 10.1016/j.mcn.2008.07.026. Epub, 2008 Aug 15. PMID:18775496 doi:http://dx.doi.org/10.1016/j.mcn.2008.07.026
  21. ↑ McCroskery S, Bailey A, Lin L, Daniels MP. Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures. Neuroscience. 2009 Sep 29;163(1):168-79. doi: 10.1016/j.neuroscience.2009.06.012., Epub 2009 Jun 10. PMID:19524020 doi:http://dx.doi.org/10.1016/j.neuroscience.2009.06.012
  22. ↑ Lin L, McCroskery S, Ross JM, Chak Y, Neuhuber B, Daniels MP. Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases. Exp Cell Res. 2010 Aug 15;316(14):2260-77. doi: 10.1016/j.yexcr.2010.05.006. Epub, 2010 May 13. PMID:20471381 doi:http://dx.doi.org/10.1016/j.yexcr.2010.05.006
  23. ↑ Tseng CN, Zhang L, Wu SL, Wang WF, Wang ZZ, Cascio M. Asparagine of z8 insert is critical for the affinity, conformation, and acetylcholine receptor-clustering activity of neural agrin. J Biol Chem. 2010 Sep 3;285(36):27641-51. doi: 10.1074/jbc.M110.130625. Epub 2010, Jun 21. PMID:20566625 doi:http://dx.doi.org/10.1074/jbc.M110.130625
  24. ↑ Banyai L, Sonderegger P, Patthy L. Agrin binds BMP2, BMP4 and TGFbeta1. PLoS One. 2010 May 21;5(5):e10758. doi: 10.1371/journal.pone.0010758. PMID:20505824 doi:http://dx.doi.org/10.1371/journal.pone.0010758
  25. ↑ Ferns MJ, Campanelli JT, Hoch W, Scheller RH, Hall Z. The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron. 1993 Sep;11(3):491-502. PMID:8398142
  26. ↑ Glass DJ, Bowen DC, Stitt TN, Radziejewski C, Bruno J, Ryan TE, Gies DR, Shah S, Mattsson K, Burden SJ, DiStefano PS, Valenzuela DM, DeChiara TM, Yancopoulos GD. Agrin acts via a MuSK receptor complex. Cell. 1996 May 17;85(4):513-23. PMID:8653787
  27. ↑ O'Toole JJ, Deyst KA, Bowe MA, Nastuk MA, McKechnie BA, Fallon JR. Alternative splicing of agrin regulates its binding to heparin alpha-dystroglycan, and the cell surface. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7369-74. PMID:8693000
  28. ↑ Kim ML, Chandrasekharan K, Glass M, Shi S, Stahl MC, Kaspar B, Stanley P, Martin PT. O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors. Mol Cell Neurosci. 2008 Nov;39(3):452-64. doi: 10.1016/j.mcn.2008.07.026. Epub, 2008 Aug 15. PMID:18775496 doi:http://dx.doi.org/10.1016/j.mcn.2008.07.026
  29. ↑ McCroskery S, Bailey A, Lin L, Daniels MP. Transmembrane agrin regulates dendritic filopodia and synapse formation in mature hippocampal neuron cultures. Neuroscience. 2009 Sep 29;163(1):168-79. doi: 10.1016/j.neuroscience.2009.06.012., Epub 2009 Jun 10. PMID:19524020 doi:http://dx.doi.org/10.1016/j.neuroscience.2009.06.012
  30. ↑ Lin L, McCroskery S, Ross JM, Chak Y, Neuhuber B, Daniels MP. Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases. Exp Cell Res. 2010 Aug 15;316(14):2260-77. doi: 10.1016/j.yexcr.2010.05.006. Epub, 2010 May 13. PMID:20471381 doi:http://dx.doi.org/10.1016/j.yexcr.2010.05.006
  31. ↑ Tseng CN, Zhang L, Wu SL, Wang WF, Wang ZZ, Cascio M. Asparagine of z8 insert is critical for the affinity, conformation, and acetylcholine receptor-clustering activity of neural agrin. J Biol Chem. 2010 Sep 3;285(36):27641-51. doi: 10.1074/jbc.M110.130625. Epub 2010, Jun 21. PMID:20566625 doi:http://dx.doi.org/10.1074/jbc.M110.130625
  32. ↑ Banyai L, Sonderegger P, Patthy L. Agrin binds BMP2, BMP4 and TGFbeta1. PLoS One. 2010 May 21;5(5):e10758. doi: 10.1371/journal.pone.0010758. PMID:20505824 doi:http://dx.doi.org/10.1371/journal.pone.0010758
  33. ↑ Zong Y, Zhang B, Gu S, Lee K, Zhou J, Yao G, Figueiredo D, Perry K, Mei L, Jin R. Structural basis of agrin-LRP4-MuSK signaling. Genes Dev. 2012 Feb 1;26(3):247-58. doi: 10.1101/gad.180885.111. PMID:22302937 doi:10.1101/gad.180885.111

3v65, resolution 3.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3v65&oldid=3594159"