1RH7
Crystal Structure of Resistin-like beta
Summary for 1RH7
| Entry DOI | 10.2210/pdb1rh7/pdb |
| Related | 1RFX 1RGX |
| Descriptor | Resistin-like beta, PLATINUM (II) ION, HEXAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | hormone; glucose uptake; resistin/fizz family, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, hormone-growth factor complex, hormone/growth factor |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 6 |
| Total formula weight | 53592.63 |
| Authors | Patel, S.D.,Rajala, M.W.,Scherer, P.E.,Shapiro, L.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-11-13, release date: 2004-06-08, Last modification date: 2024-10-30) |
| Primary citation | Patel, S.D.,Rajala, M.W.,Rossetti, L.,Scherer, P.E.,Shapiro, L. Disulfide-dependent multimeric assembly of resistin family hormones Science, 304:1154-1158, 2004 Cited by PubMed Abstract: Resistin, founding member of the resistin-like molecule (RELM) hormone family, is secreted selectively from adipocytes and induces liver-specific antagonism of insulin action, thus providing a potential molecular link between obesity and diabetes. Crystal structures of resistin and RELMbeta reveal an unusual multimeric structure. Each protomer comprises a carboxy-terminal disulfide-rich beta-sandwich "head" domain and an amino-terminal alpha-helical "tail" segment. The alpha-helical segments associate to form three-stranded coiled coils, and surface-exposed interchain disulfide linkages mediate the formation of tail-to-tail hexamers. Analysis of serum samples shows that resistin circulates in two distinct assembly states, likely corresponding to hexamers and trimers. Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in pancreatic-insulin clamp studies reveals substantially more potent effects on hepatic insulin sensitivity than those observed with wild-type resistin. This result suggests that processing of the intertrimer disulfide bonds may reflect an obligatory step toward activation. PubMed: 15155948DOI: 10.1126/science.1093466 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.106 Å) |
Structure validation
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