人胰岛素受体酪氨酸激酶结构域的晶体结构
Crystal structure of the tyrosine kinase domain of the human insulin receptor.
作者信息
Hubbard S R, Wei L, Ellis L, Hendrickson W A
机构信息
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
出版信息
Nature. 1994;372(6508):746-54. doi: 10.1038/372746a0.
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 A 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.
人类胰岛素受体酪氨酸激酶结构域的X射线晶体结构已通过多波长反常衍射相位法确定，并精修至2.1埃分辨率。该结构揭示了对酪氨酸而非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，即响应胰岛素而自磷酸化的酪氨酸之一Tyr 1162结合在活性位点中。
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