5UV6
Crystal structure of human Opioid Binding Protein/Cell Adhesion Molecule Like (OPCML)
Summary for 5UV6
| Entry DOI | 10.2210/pdb5uv6/pdb |
| Descriptor | Opioid-binding protein/cell adhesion molecule, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | gpi-anchored ig domain cell adhesion molecule, cell adhesion |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 65309.34 |
| Authors | Birtley, J.R.,Stern, L.J.,Gabra, H.,Zanini, E. (deposition date: 2017-02-19, release date: 2018-03-21, Last modification date: 2024-11-06) |
| Primary citation | Birtley, J.R.,Alomary, M.,Zanini, E.,Antony, J.,Maben, Z.,Weaver, G.C.,Von Arx, C.,Mura, M.,Marinho, A.T.,Lu, H.,Morecroft, E.V.N.,Karali, E.,Chayen, N.E.,Tate, E.W.,Jurewicz, M.,Stern, L.J.,Recchi, C.,Gabra, H. Inactivating mutations and X-ray crystal structure of the tumor suppressor OPCML reveal cancer-associated functions. Nat Commun, 10:3134-3134, 2019 Cited by PubMed Abstract: 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 Å 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. PubMed: 31316070DOI: 10.1038/s41467-019-10966-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65001977608 Å) |
Structure validation
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