5xwx
From Proteopedia
(Difference between revisions)
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<StructureSection load='5xwx' size='340' side='right' caption='[[5xwx]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='5xwx' size='340' side='right' caption='[[5xwx]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5xwx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XWX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XWX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xwx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XWX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XWX FirstGlance]. <br> |
| - | </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=5xwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xwx OCA], [http://pdbe.org/5xwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xwx RCSB], [http://www.ebi.ac.uk/pdbsum/5xwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xwx ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sdk1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5xwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xwx OCA], [http://pdbe.org/5xwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xwx RCSB], [http://www.ebi.ac.uk/pdbsum/5xwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xwx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SDK1_MOUSE SDK1_MOUSE]] Adhesion molecule that promotes lamina-specific synaptic connections in the retina. Expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions.[UniProtKB:Q8AV58] | [[http://www.uniprot.org/uniprot/SDK1_MOUSE SDK1_MOUSE]] Adhesion molecule that promotes lamina-specific synaptic connections in the retina. Expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions.[UniProtKB:Q8AV58] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cell-cell adhesion is important for cell growth, tissue development, and neural network formation. Structures of cell adhesion molecules have been widely studied by crystallography, revealing the molecular details of adhesion interfaces. However, due to technical limitations, the overall structure and organization of adhesion molecules at cell adhesion interfaces has not been fully investigated. Here, we combine electron microscopy and other biophysical methods to characterize the structure of cell-cell adhesion mediated by the cell adhesion molecule Sidekick (Sidekick-1 and Sidekick-2) and obtain 3D views of the Sidekick-mediated adhesion interfaces as well as the organization of Sidekick molecules between cell membranes by electron tomography. The results suggest that the Ig-like domains and the fibronectin III (FnIII) domains of Sidekicks play different roles in cell adhesion. The Ig-like domains mediate the homophilic transinteractions bridging adjacent cells, while the FnIII domains interact with membranes, resulting in a tight adhesion interface between cells that may contribute to the specificity and plasticity of cell-cell contacts during cell growth and neural development. | ||
| + | |||
| + | Architecture of cell-cell adhesion mediated by sidekicks.,Tang H, Chang H, Dong Y, Guo L, Shi X, Wu Y, Huang Y, He Y Proc Natl Acad Sci U S A. 2018 Sep 11;115(37):9246-9251. doi:, 10.1073/pnas.1801810115. Epub 2018 Aug 27. PMID:30150416<ref>PMID:30150416</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5xwx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Lk3 transgenic mice]] | ||
[[Category: Dong, Y]] | [[Category: Dong, Y]] | ||
[[Category: He, Y]] | [[Category: He, Y]] | ||
Current revision
Crystal structure of the four N-terminal immunoglogulin domains of Sidekick-1 protein
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