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1rgx
From Proteopedia
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Crystal Structure of resisitin
Overview
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.
About this Structure
1RGX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Disulfide-dependent multimeric assembly of resistin family hormones., Patel SD, Rajala MW, Rossetti L, Scherer PE, Shapiro L, Science. 2004 May 21;304(5674):1154-8. PMID:15155948
Page seeded by OCA on Wed Nov 21 01:35:18 2007
Categories: Mus musculus | Single protein | Burley, S.K. | NYSGXRC, New.York.Structural.GenomiX.Research.Consortium. | Patel, S.D. | Rajala, M.W. | Scherer, P.E. | Shapiro, L. | Hormone; glucose uptake; resistin/fizz family | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
