1jb3: Difference between revisions

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-[[Image:1jb3.png|left|200px]]
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+==The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1==
-The line below this paragraph, containing "STRUCTURE_1jb3", creates the "Structure Box" on the page.
+<StructureSection load='1jb3' size='340' side='right'caption='[[1jb3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1jb3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JB3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jb3 OCA], [https://pdbe.org/1jb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jb3 RCSB], [https://www.ebi.ac.uk/pdbsum/1jb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jb3 ProSAT]</span></td></tr>
-{{STRUCTURE_1jb3|  PDB=1jb3  |  SCENE=  }}
+</table>
+== Function ==
-===The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1===
+[https://www.uniprot.org/uniprot/AGRIN_CHICK AGRIN_CHICK] 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. 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 funtion 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.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>   Isoform 9: transmembrane agrin (TM-agrin), the predominant 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:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>   Isoform 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>   Isoform 5: muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>   Agrin N-terminal 110 kDa subunit: is involved in modulation of growth factor signaling (By similarity). Involved also in the 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.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</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 'B' splice variants of this fragment also show an increase in the number of filopodia.<ref>PMID:7860635</ref> <ref>PMID:11425874</ref> <ref>PMID:15198666</ref> <ref>PMID:17012237</ref> <ref>PMID:17649979</ref> <ref>PMID:19940118</ref> <ref>PMID:22984437</ref>
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-The line below this paragraph, {{ABSTRACT_PUBMED_11473262}}, adds the Publication Abstract to the page
-(as it appears on PubMed at http://www.pubmed.gov), where 11473262 is the PubMed ID number.
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-{{ABSTRACT_PUBMED_11473262}}
-==About this Structure==
-[[1jb3]] is a 1 chain structure of [[Agrin]] with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JB3 OCA].
 ==See Also==
-*[[Agrin]]
+*[[Agrin 3D structures|Agrin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:11473262</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Stetefeld, J.]]
+[[Category: Large Structures]]
-[[Category: Agrin]]
+[[Category: Stetefeld J]]
-[[Category: Cell adhesion]]
-[[Category: Interaction coiled-doil proteins with globular protein]]
-[[Category: Neuromuscular junction]]
-[[Category: Ob-fold]]
-[[Category: Timp]]