4ofp: Difference between revisions
New page: '''Unreleased structure''' The entry 4ofp is ON HOLD Authors: Ozkan, E., Garcia, K.C. Description: Crystal Structure of SYG-2 D3-D4 |
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==Crystal Structure of SYG-2 D3-D4== | |||
<StructureSection load='4ofp' size='340' side='right'caption='[[4ofp]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ofp]] 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=4OFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OFP 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]] 3Å</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></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=4ofp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ofp OCA], [https://pdbe.org/4ofp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ofp RCSB], [https://www.ebi.ac.uk/pdbsum/4ofp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ofp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SYG2_CAEEL SYG2_CAEEL] Cell adhesion protein (PubMed:15035988). Determines synapse formation (PubMed:15035988, PubMed:21858180, PubMed:24485456). Required for correct localization of syg-1 at synaptic sites (PubMed:15035988).<ref>PMID:15035988</ref> <ref>PMID:21858180</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: | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ofp" 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 20:12, 20 September 2023
Crystal Structure of SYG-2 D3-D4Crystal Structure of SYG-2 D3-D4
Structural highlights
FunctionSYG2_CAEEL Cell adhesion protein (PubMed:15035988). Determines synapse formation (PubMed:15035988, PubMed:21858180, PubMed:24485456). Required for correct localization of syg-1 at synaptic sites (PubMed:15035988).[1] [2] [3] Publication Abstract from PubMedSYG-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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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