IDENTIFICATION OF A 10-AMINO ACID PROLINE-RICH SH3 BINDING-SITE
IDENTIFICATION OF A 10-AMINO ACID PROLINE-RICH SH3 BINDING-SITE
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DOI：
10.1126/science.8438166
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发表时间：
1993-02-19
期刊：
影响因子：
56.9
通讯作者：
BALTIMORE, D
中科院分区：
文献类型：
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作者：
REN, RB;MAYER, BJ;BALTIMORE, D
Src同源3(SH3)区是一个很小的蛋白质结构域，存在于一大组蛋白质中，包括细胞骨架元件和信号蛋白。SH3结构域被认为是介导蛋白质-蛋白质关联的模块，并与Src同源2(SH2)结构域一起调节细胞质信号。两个SH3结合蛋白的SH3结合位点被定位在一个富含脯氨酸残基的九个或十个氨基酸的伸展区域。类似的SH3结合基序存在于福尔马林中，福尔马林是一种在小鼠胚胎肢体中起模式形成作用的蛋白质，也是M胆碱型乙酰胆碱受体的一个亚型。SH3结合位点的鉴定为理解SH3结构域与其靶标之间的相互作用提供了基础。
The Src homology 3 (SH3) region is a small protein domain present in a very large group of proteins, including cytoskeletal elements and signaling proteins. It is believed that SH3 domains serve as modules that mediate protein-protein associations and, along with Src homology 2 (SH2) domains, regulate cytoplasmic signaling. The SH3 binding sites of two SH3 binding proteins were localized to a nine- or ten-amino acid stretch very rich in proline residues. Similar SH3 binding motifs exist in the formins, proteins that function in pattern formation in embryonic limbs of the mouse, and one subtype of the muscarinic acetylcholine receptor. Identification of the SH3 binding site provides a basis for understanding the interaction between the SH3 domains and their targets.