3r0n
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==Crystal Structure of the Immunoglobulin variable domain of Nectin-2== |
+ | <StructureSection load='3r0n' size='340' side='right' caption='[[3r0n]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3r0n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R0N FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HVEB, PRR2, PVRL2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3r0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r0n RCSB], [http://www.ebi.ac.uk/pdbsum/3r0n PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/PVRL2_HUMAN PVRL2_HUMAN]] Probable cell adhesion protein.<ref>PMID:9657005</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Nectins are members of the Ig superfamily that mediate cell-cell adhesion through homophilic and heterophilic interactions. We have determined the crystal structure of the nectin-2 homodimer at 1.3 A resolution. Structural analysis and complementary mutagenesis studies reveal the basis for recognition and selectivity among the nectin family members. Notably, the close proximity of charged residues at the dimer interface is a major determinant of the binding affinities associated with homophilic and heterophilic interactions within the nectin family. Our structural and biochemical data provide a mechanistic basis to explain stronger heterophilic versus weaker homophilic interactions among these family members and also offer insights into nectin-mediated transinteractions between engaging cells. | ||
- | + | Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion.,Samanta D, Ramagopal UA, Rubinstein R, Vigdorovich V, Nathenson SG, Almo SC Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14836-40. Epub 2012 Aug 27. PMID:22927415<ref>PMID:22927415</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | + | </StructureSection> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Almo, S C | + | [[Category: Almo, S C]] |
- | [[Category: IFN, Atoms-to-Animals:.The Immune Function Network | + | [[Category: IFN, Atoms-to-Animals:.The Immune Function Network]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: Nathenson, S G | + | [[Category: Nathenson, S G]] |
- | [[Category: Ramagopal, U A | + | [[Category: Ramagopal, U A]] |
- | [[Category: Samanta, D | + | [[Category: Samanta, D]] |
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Cell-adhesion molecule]] | [[Category: Cell-adhesion molecule]] | ||
[[Category: Ig-domain]] | [[Category: Ig-domain]] | ||
- | [[Category: New york structural genomics research consortium]] | ||
[[Category: Nysgrc]] | [[Category: Nysgrc]] | ||
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
- | [[Category: Structural genomic]] | ||
[[Category: Virus entry receptor]] | [[Category: Virus entry receptor]] |
Revision as of 21:14, 24 December 2014
Crystal Structure of the Immunoglobulin variable domain of Nectin-2
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