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X连锁无丙种球蛋白血症中SH2结构域突变的结构基础。

Structural basis of SH2 domain mutations in X-linked agammaglobulinemia.

作者信息

Vihinen M, Nilsson L, Smith C I

机构信息

Center for Structural Biochemistry, Karolinska Institute, NOVUM, Huddinge, Sweden.

出版信息

Biochem Biophys Res Commun. 1994 Dec 15;205(2):1270-7. doi: 10.1006/bbrc.1994.2802.

Abstract

The three-dimensional structure of Bruton's agammaglobulinemia tyrosine kinase (Btk) SH2 domain was modeled based on v-Src. Btk SH2 is presumably very related to the other SH2 structures consisting of two beta-sheets surrounded by two alpha-helices, with a well conserved hydrophobic core and phoshotyrosyl peptide binding site. The model was used to predict the recognition sequence of the target protein, which probably is YEXI/L. Mutations in the Btk sequence can cause the human disease X-linked agammaglobulinemia and reasons for the disease in Btk SH2 mutations were inferred from the model.

摘要

基于v-Src对布鲁顿无丙种球蛋白血症酪氨酸激酶(Btk)的SH2结构域进行了三维结构建模。Btk的SH2结构可能与其他由两个β折叠片层被两个α螺旋包围的SH2结构密切相关,具有保守的疏水核心和磷酸酪氨酸肽结合位点。该模型用于预测靶蛋白的识别序列,其可能为YEXI/L。Btk序列中的突变可导致人类疾病X连锁无丙种球蛋白血症,并从该模型推断出Btk SH2突变导致该疾病的原因。

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