5uv6
From Proteopedia
(Difference between revisions)
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==Crystal structure of human Opioid Binding Protein/Cell Adhesion Molecule Like (OPCML)== | ==Crystal structure of human Opioid Binding Protein/Cell Adhesion Molecule Like (OPCML)== | ||
- | <StructureSection load='5uv6' size='340' side='right' caption='[[5uv6]], [[Resolution|resolution]] 2.65Å' scene=''> | + | <StructureSection load='5uv6' size='340' side='right'caption='[[5uv6]], [[Resolution|resolution]] 2.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5uv6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UV6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uv6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UV6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OPCML, IGLON1, OBCAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5uv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uv6 OCA], [http://pdbe.org/5uv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uv6 RCSB], [http://www.ebi.ac.uk/pdbsum/5uv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uv6 ProSAT]</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=5uv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uv6 OCA], [http://pdbe.org/5uv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uv6 RCSB], [http://www.ebi.ac.uk/pdbsum/5uv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uv6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/OPCM_HUMAN OPCM_HUMAN]] Binds opioids in the presence of acidic lipids; probably involved in cell contact. | [[http://www.uniprot.org/uniprot/OPCM_HUMAN OPCM_HUMAN]] Binds opioids in the presence of acidic lipids; probably involved in cell contact. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | OPCML, a tumor suppressor gene, is frequently silenced epigenetically in ovarian and other cancers. Here we report, by analysis of databases of tumor sequences, the observation of OPCML somatic missense mutations from various tumor types and the impact of these mutations on OPCML function, by solving the X-ray crystal structure of this glycoprotein to 2.65 A resolution. OPCML consists of an extended arrangement of three immunoglobulin-like domains and homodimerizes via a network of contacts between membrane-distal domains. We report the generation of a panel of OPCML variants with representative clinical mutations and demonstrate clear phenotypic effects in vitro and in vivo including changes to anchorage-independent growth, interaction with activated cognate receptor tyrosine kinases, cellular migration, invasion in vitro and tumor growth in vivo. Our results suggest that clinically occurring somatic missense mutations in OPCML have the potential to contribute to tumorigenesis in a variety of cancers. | ||
+ | |||
+ | Inactivating mutations and X-ray crystal structure of the tumor suppressor OPCML reveal cancer-associated functions.,Birtley JR, Alomary M, Zanini E, Antony J, Maben Z, Weaver GC, Von Arx C, Mura M, Marinho AT, Lu H, Morecroft EVN, Karali E, Chayen NE, Tate EW, Jurewicz M, Stern LJ, Recchi C, Gabra H Nat Commun. 2019 Jul 17;10(1):3134. doi: 10.1038/s41467-019-10966-8. PMID:31316070<ref>PMID:31316070</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5uv6" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Birtley, J R]] | [[Category: Birtley, J R]] | ||
[[Category: Gabra, H]] | [[Category: Gabra, H]] |
Revision as of 06:40, 31 July 2019
Crystal structure of human Opioid Binding Protein/Cell Adhesion Molecule Like (OPCML)
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