SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85-ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE
SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85-ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE
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DOI：
10.1016/0092-8674(93)90259-s
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发表时间：
1993-05-21
期刊：
影响因子：
64.5
通讯作者：
CAMPBELL, ID
中科院分区：
文献类型：
--
作者：
BOOKER, GW;GOUT, I;CAMPBELL, ID
SH3结构域存在于与受体酪氨酸激酶信号转导复合物相关的蛋白质中。磷脂酰肌醇3-激酶85 kd调控亚基的SH3结构域的溶液结构被证明是一个紧凑的β桶，由5条β链组成，排列在3条和2条的β片上。该结构与鸡脑α谱蛋白相似，但代表了不同的SH3结构域，在第二和第三β链之间插入可能影响结合特异性。由sh3结合蛋白动力蛋白衍生的合成肽形成复合物引起的H-1化学位移变化，以及氨基酸序列比较表明，配体结合位点由两个带电环两侧的疏水表面组成。
SH3 domains are found in proteins associated with receptor tyrosine kinase signal transduction complexes. The solution structure of the SH3 domain of the 85 kd regulatory subunit of phosphatidylinositol 3-kinase is shown to be a compact beta barrel consisting of five beta strands arranged in two beta sheets of three and two strands. The structure is similar to that of chicken brain alpha spectrin but represents a distinct class of SH3 domain, with an insertion between the second and third beta strands that may influence binding specificity. H-1 chemical shift changes induced by complex formation with a synthetic peptide derived from the SH3-binding protein dynamin, together with amino acid sequence comparisons, suggest that the ligand-binding site consists of a hydrophobic surface flanked by two charged loops.