CRYSTAL-STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN-RECEPTOR

被引：939

作者：

HUBBARD, SR

WEI, L

ELIS, L

HENDRICKSON, WA

机构：

[1] COLUMBIA UNIV,HOWARD HUGHES MED INST,NEW YORK,NY 10032

[2] TEXAS A&M UNIV,INST BIOSCI & TECHNOL,WM KECK CTR GENOME INFORMAT,HOUSTON,TX 77030

来源：

NATURE | 1994年 / 372卷 / 6508期

关键词：

D O I：

10.1038/372746a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 Angstrom resolution. The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.

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页码：746 / 754

页数：9

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