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| {{STRUCTURE_1rh7| PDB=1rh7 | SCENE= }} | | {{STRUCTURE_1rh7| PDB=1rh7 | SCENE= }} |
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| '''Crystal Structure of Resistin-like beta'''
| | ===Crystal Structure of Resistin-like beta=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15155948}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15155948 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15155948}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Resistin/fizz family]] | | [[Category: Resistin/fizz family]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:29:40 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:40:53 2008'' |
