3r0n
From Proteopedia
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| - | [[Image:3r0n.png|left|200px]] | ||
| - | + | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3R0N 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]] 1.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3r0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0n OCA], [https://pdbe.org/3r0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r0n RCSB], [https://www.ebi.ac.uk/pdbsum/3r0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | ||
| + | <div class="pdbe-citations 3r0n" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Poliovirus receptor-related protein|Poliovirus receptor-related protein]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Almo SC]] |
| - | + | [[Category: Nathenson SG]] | |
| - | [[Category: Nathenson | + | [[Category: Ramagopal UA]] |
| - | [[Category: Ramagopal | + | [[Category: Samanta D]] |
| - | [[Category: Samanta | + | |
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Current revision
Crystal Structure of the Immunoglobulin variable domain of Nectin-2
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