1RGX

Crystal Structure of resisitin

1RGX の概要

• エントリーDOI: 10.2210/pdb1rgx/pdb
• 関連するPDBエントリー: 1RFX 1RH7
• 分子名称: Resistin (2 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 37514.01

構造登録者

Patel, S.D.,Rajala, M.W.,Scherer, P.E.,Shapiro, L.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2003-11-13, 公開日: 2004-06-08, 最終更新日: 2024-11-13)

主引用文献

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

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: 15155948
DOI: 10.1126/science.1093466

実験手法

X-RAY DIFFRACTION (1.787 Å)