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| | ==Crystal Structure of SYG-1 D1, Crystal form 1== | | ==Crystal Structure of SYG-1 D1, Crystal form 1== |
| - | <StructureSection load='4of6' size='340' side='right' caption='[[4of6]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4of6' size='340' side='right'caption='[[4of6]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4of6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OF6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OF6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4of6]] is a 2 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=4OF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OF6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4of0|4of0]], [[4of3|4of3]], [[4of7|4of7]], [[4of8|4of8]], [[4ofd|4ofd]], [[4ofi|4ofi]], [[4ofk|4ofk]], [[4ofp|4ofp]], [[4ofy|4ofy]]</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=4of6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4of6 OCA], [https://pdbe.org/4of6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4of6 RCSB], [https://www.ebi.ac.uk/pdbsum/4of6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4of6 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CELE_K02E10.8, K02E10.8, syg-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4of6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4of6 OCA], [http://pdbe.org/4of6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4of6 RCSB], [http://www.ebi.ac.uk/pdbsum/4of6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4of6 ProSAT]</span></td></tr> | + | |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: Garcia, K C]] | + | [[Category: Large Structures]] |
| - | [[Category: Ozkan, E]] | + | [[Category: Garcia KC]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Ozkan E]] |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Immunoglobulin superfamily]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: N-linked glycosylation]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Synaptogenesis]]
| + | |
| Structural highlights
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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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