AN ALTERNATIVE TO SH2 DOMAINS FOR BINDING TYROSINE-PHOSPHORYLATED PROTEINS
AN ALTERNATIVE TO SH2 DOMAINS FOR BINDING TYROSINE-PHOSPHORYLATED PROTEINS
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DOI：
10.1126/science.7527937
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发表时间：
1994-12-16
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;WILLIAMS, LT
Src同源2（SH 2）结构域特异性结合酪氨酸磷酸化蛋白，参与生长因子和癌基因的信号传导。一个蛋白质结构域被鉴定为特异性结合其靶蛋白的酪氨酸磷酸化形式，但不同于已知的SH 2序列。磷酸酪氨酸结合（PTB）结构域被发现在两种蛋白质：SHC，一种蛋白质参与信号通过Ras;和SCK，由以前未知的基因编码。PTB结构域的SHC特异性结合酪氨酸磷酸化的145千道尔顿蛋白。PTB结构域是SH 2结构域的替代物，用于特异性地将酪氨酸磷酸化的蛋白质募集到信号传导复合物中，并且可能通过许多生长因子参与信号传导。
Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that participate in signaling by growth factors and oncogenes. A protein domain was identified that bound specifically to the tyrosine-phosphorylated form of its target protein but differs from known SH2 sequences. Phosphotyrosine-binding (PTB) domains were found in two proteins: SHC, a protein implicated in signaling through Ras; and SCK, encoded by a previously uncharacterized gene. The PTB domain of SHC specifically bound to a tyrosine-phosphorylated 145-kilodalton protein. PTB domains are an alternative to SH2 domains for specifically recruiting tyrosine-phosphorylated proteins into signaling complexes and are likely to take part in signaling by many growth factors.