1rh7

File:1rh7.gif

spinqualitylabelsall models 1rh7, resolution 3.106Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Resistin-like beta

OverviewOverview

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 StructureAbout this Structure

1RH7 is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 14:50:51 2008