CRYSTAL-STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN-RECEPTOR
CRYSTAL-STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN-RECEPTOR
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DOI：
10.1038/372746a0
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发表时间：
1994-12-22
期刊：
影响因子：
64.8
通讯作者：
HENDRICKSON, WA
中科院分区：
文献类型：
--
作者：
HUBBARD, SR;WEI, L;HENDRICKSON, WA
用多波长异常衍射相位法测定了人胰岛素受体酪氨酸激酶结构域的x射线晶体结构，并将其细化到2.1埃分辨率。该结构揭示了对酪氨酸而不是丝氨酸或苏氨酸的底物偏好的决定因素，以及一种新的自抑制机制，其中一种酪氨酸在胰岛素反应中被自磷酸化，Tyr 1162结合在活性位点。
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.