晶体结构的细胞外段整合素αVbeta3。
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熊JP, Stehle T, Diefenbach B,张R, Dunker R,斯科特•DL Joachimiak,古德曼SL, Arnaout MA
晶体结构的细胞外段整合素αVbeta3。
科学。2001年10月12日,294 (5541):339 - 45。Epub 2001年9月6日。
- PubMed ID
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11546839 (在PubMed]
- 文摘
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整合蛋白是alphabeta heterodimeric受体调节二阶cation-dependent信息并通过严格监管cell-matrix附着力与配体的相互作用。我们已经解决了晶体结构的整合素的细胞外部分alphaVbeta3 3.1一项决议。12域组装成一个卵形的“头部”和两个“尾巴”。In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation. The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins. A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.