4y89
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y88|4y88]], [[4y8a|4y8a]], [[4y8b|4y8b]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y88|4y88]], [[4y8a|4y8a]], [[4y8b|4y8b]]</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=4y89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y89 RCSB], [http://www.ebi.ac.uk/pdbsum/4y89 PDBsum]</span></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=4y89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y89 OCA], [http://pdbe.org/4y89 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y89 RCSB], [http://www.ebi.ac.uk/pdbsum/4y89 PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CEACAM7 is a human cellular adhesion protein that is expressed on the surface of colon and rectum epithelial cells and is downregulated in colorectal cancers. It achieves cell adhesion through dimerization of the N-terminal IgV domain. The crystal structure of the N-terminal dimerization domain of CEACAM has been determined at 1.47 A resolution. The overall fold of CEACAM7 is similar to those of CEACAM1 and CEACAM5; however, there are differences, the most notable of which is an insertion that causes the C'' strand to buckle, leading to the creation of a hydrogen bond in the dimerization interface. The Kdimerization for CEACAM7 determined by sedimentation equilibrium is tenfold tighter than that measured for CEACAM5. These findings suggest that the dimerization affinities of CEACAMs are modulated via sequence variation in the dimerization surface. | ||
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| + | Structure of the N-terminal dimerization domain of CEACAM7.,Bonsor DA, Beckett D, Sundberg EJ Acta Crystallogr F Struct Biol Commun. 2015 Sep 1;71(Pt 9):1169-75. doi:, 10.1107/S2053230X15013576. Epub 2015 Aug 25. PMID:26323304<ref>PMID:26323304</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4y89" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:05, 30 September 2015
Crystal structure of the N-terminal domain of CEACAM7
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