4of7: Difference between revisions

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New page: '''Unreleased structure''' The entry 4of7 is ON HOLD Authors: Ozkan, E., Garcia, K.C. Description: Crystal Structure of SYG-1 D1, Crystal Form 2
 
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'''Unreleased structure'''


The entry 4of7 is ON HOLD
==Crystal Structure of SYG-1 D1, Crystal Form 2==
<StructureSection load='4of7' size='340' side='right'caption='[[4of7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4of7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OF7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4of7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4of7 OCA], [https://pdbe.org/4of7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4of7 RCSB], [https://www.ebi.ac.uk/pdbsum/4of7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4of7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYG1_CAEEL SYG1_CAEEL] Cell adhesion protein (PubMed:15035988). Involved in synapse formation in the HSNL egg-laying motor neuron (PubMed:12628183, PubMed:15035988, PubMed:21858180, PubMed:24485456). Inhibits assembly of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and protects them from elimination (PubMed:17626846). Also required for F-actin assembly at the synaptic region and for axon branch formation (PubMed:24439377).<ref>PMID:12628183</ref> <ref>PMID:15035988</ref> <ref>PMID:17626846</ref> <ref>PMID:21858180</ref> <ref>PMID:24439377</ref> <ref>PMID:24485456</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SYG-1 and SYG-2 are multipurpose cell adhesion molecules (CAMs) that have evolved across all major animal taxa to participate in diverse physiological functions, ranging from synapse formation to formation of the kidney filtration barrier. In the crystal structures of several SYG-1 and SYG-2 orthologs and their complexes, we find that SYG-1 orthologs homodimerize through a common, bispecific interface that similarly mediates an unusual orthogonal docking geometry in the heterophilic SYG-1/SYG-2 complex. C. elegans SYG-1's specification of proper synapse formation in vivo closely correlates with the heterophilic complex affinity, which appears to be tuned for optimal function. Furthermore, replacement of the interacting domains of SYG-1 and SYG-2 with those from CAM complexes that assume alternative docking geometries or the introduction of segmental flexibility compromised synaptic function. These results suggest that SYG extracellular complexes do not simply act as "molecular velcro" and that their distinct structural features are important in instructing synaptogenesis. PAPERFLICK:


Authors: Ozkan, E., Garcia, K.C.
Extracellular Architecture of the SYG-1/SYG-2 Adhesion Complex Instructs Synaptogenesis.,Ozkan E, Chia PH, Wang RR, Goriatcheva N, Borek D, Otwinowski Z, Walz T, Shen K, Garcia KC Cell. 2014 Jan 30;156(3):482-94. doi: 10.1016/j.cell.2014.01.004. PMID:24485456<ref>PMID:24485456</ref>


Description: Crystal Structure of SYG-1 D1, Crystal Form 2
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4of7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Garcia KC]]
[[Category: Ozkan E]]

Latest revision as of 20:11, 20 September 2023

Crystal Structure of SYG-1 D1, Crystal Form 2Crystal Structure of SYG-1 D1, Crystal Form 2

Structural highlights

4of7 is a 4 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYG1_CAEEL Cell adhesion protein (PubMed:15035988). Involved in synapse formation in the HSNL egg-laying motor neuron (PubMed:12628183, PubMed:15035988, PubMed:21858180, PubMed:24485456). Inhibits assembly of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and protects them from elimination (PubMed:17626846). Also required for F-actin assembly at the synaptic region and for axon branch formation (PubMed:24439377).[1] [2] [3] [4] [5] [6]

Publication Abstract from PubMed

SYG-1 and SYG-2 are multipurpose cell adhesion molecules (CAMs) that have evolved across all major animal taxa to participate in diverse physiological functions, ranging from synapse formation to formation of the kidney filtration barrier. In the crystal structures of several SYG-1 and SYG-2 orthologs and their complexes, we find that SYG-1 orthologs homodimerize through a common, bispecific interface that similarly mediates an unusual orthogonal docking geometry in the heterophilic SYG-1/SYG-2 complex. C. elegans SYG-1's specification of proper synapse formation in vivo closely correlates with the heterophilic complex affinity, which appears to be tuned for optimal function. Furthermore, replacement of the interacting domains of SYG-1 and SYG-2 with those from CAM complexes that assume alternative docking geometries or the introduction of segmental flexibility compromised synaptic function. These results suggest that SYG extracellular complexes do not simply act as "molecular velcro" and that their distinct structural features are important in instructing synaptogenesis. PAPERFLICK:

Extracellular Architecture of the SYG-1/SYG-2 Adhesion Complex Instructs Synaptogenesis.,Ozkan E, Chia PH, Wang RR, Goriatcheva N, Borek D, Otwinowski Z, Walz T, Shen K, Garcia KC Cell. 2014 Jan 30;156(3):482-94. doi: 10.1016/j.cell.2014.01.004. PMID:24485456[7]

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

References

  1. ↑ Shen K, Bargmann CI. The immunoglobulin superfamily protein SYG-1 determines the location of specific synapses in C. elegans. Cell. 2003 Mar 7;112(5):619-30. doi: 10.1016/s0092-8674(03)00113-2. PMID:12628183 doi:http://dx.doi.org/10.1016/s0092-8674(03)00113-2
  2. ↑ Shen K, Fetter RD, Bargmann CI. Synaptic specificity is generated by the synaptic guidepost protein SYG-2 and its receptor, SYG-1. Cell. 2004 Mar 19;116(6):869-81. doi: 10.1016/s0092-8674(04)00251-x. PMID:15035988 doi:http://dx.doi.org/10.1016/s0092-8674(04)00251-x
  3. ↑ Ding M, Chao D, Wang G, Shen K. Spatial regulation of an E3 ubiquitin ligase directs selective synapse elimination. Science. 2007 Aug 17;317(5840):947-51. doi: 10.1126/science.1145727. Epub 2007 , Jul 12. PMID:17626846 doi:http://dx.doi.org/10.1126/science.1145727
  4. ↑ Wanner N, Noutsou F, Baumeister R, Walz G, Huber TB, Neumann-Haefelin E. Functional and spatial analysis of C. elegans SYG-1 and SYG-2, orthologs of the Neph/nephrin cell adhesion module directing selective synaptogenesis. PLoS One. 2011;6(8):e23598. doi: 10.1371/journal.pone.0023598. Epub 2011 Aug 15. PMID:21858180 doi:http://dx.doi.org/10.1371/journal.pone.0023598
  5. ↑ Chia PH, Chen B, Li P, Rosen MK, Shen K. Local F-actin network links synapse formation and axon branching. Cell. 2014 Jan 16;156(1-2):208-20. doi: 10.1016/j.cell.2013.12.009. PMID:24439377 doi:http://dx.doi.org/10.1016/j.cell.2013.12.009
  6. ↑ Ozkan E, Chia PH, Wang RR, Goriatcheva N, Borek D, Otwinowski Z, Walz T, Shen K, Garcia KC. Extracellular Architecture of the SYG-1/SYG-2 Adhesion Complex Instructs Synaptogenesis. Cell. 2014 Jan 30;156(3):482-94. doi: 10.1016/j.cell.2014.01.004. PMID:24485456 doi:http://dx.doi.org/10.1016/j.cell.2014.01.004
  7. ↑ Ozkan E, Chia PH, Wang RR, Goriatcheva N, Borek D, Otwinowski Z, Walz T, Shen K, Garcia KC. Extracellular Architecture of the SYG-1/SYG-2 Adhesion Complex Instructs Synaptogenesis. Cell. 2014 Jan 30;156(3):482-94. doi: 10.1016/j.cell.2014.01.004. PMID:24485456 doi:http://dx.doi.org/10.1016/j.cell.2014.01.004

4of7, resolution 2.10Å

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