1RFX: Crystal Structure Of Resisitin

Citation:
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.
PDB ID: 1RFXDownload
MMDB ID: 27722
PDB Deposition Date: 2003/11/10
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1RFX: trimeric; determined by author and by software (PISA)
Molecular Components in 1RFX
Label Count Molecule
Proteins (3 molecules)
3
Resistin(Gene symbol: Retn)
Molecule annotation
Chemicals (20 molecules)
1
11
2
7
3
1
4
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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