PTB DOMAIN BINDING TO SIGNALING PROTEINS THROUGH A SEQUENCE MOTIF CONTAINING PHOSPHOTYROSINE
PTB DOMAIN BINDING TO SIGNALING PROTEINS THROUGH A SEQUENCE MOTIF CONTAINING PHOSPHOTYROSINE
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DOI：
10.1126/science.7539155
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发表时间：
1995-05-26
期刊：
影响因子：
56.9
通讯作者：
WILLIAMS, LT
中科院分区：
文献类型：
--
作者：
KAVANAUGH, WM;TURCK, CW;WILLIAMS, LT
Src同源2（SH 2）结构域通过特异性结合酪氨酸磷酸化蛋白质介导信号复合物的组装。已经鉴定了磷酸酪氨酸结合（PTB）结构域，其也特异性结合酪氨酸磷酸化的靶标，但在结构上不同于SH 2结构域。表达克隆用于鉴定PTB结构域的靶标。在天冬酰胺-X（1）-X（2）-磷酸酪氨酸（其中X代表任何氨基酸）序列基序内与磷酸酪氨酸结合的PTB结构域，存在于许多信号蛋白中，不被SH 2结构域识别。突变研究表明，PTB结构域的高亲和力结合可能需要基序的特定构象。
Src homology 2 (SH2) domains mediate assembly of signaling complexes by binding specifically to tyrosine-phosphorylated proteins. A phosphotyrosine binding (PTB) domain has been identified which also binds specifically to tyrosine-phosphorylated targets, but is structurally different from SH2 domains, Expression cloning was used to identify targets of PTB domains. PTB domains bound to phosphotyrosine within a sequence motif, asparagine-X(1)-X(2)-phosphotyrosine (where X represents any amino acid), that is found in many signaling proteins and is not recognized by SH2 domains. Mutational studies indicated that high affinity binding of PTB domains may require a specific conformation of the motif.