IDENTIFICATION OF A 10-AMINO ACID PROLINE-RICH SH3 BINDING-SITE

被引:1140
作者
REN, RB [1 ]
MAYER, BJ [1 ]
CICCHETTI, P [1 ]
BALTIMORE, D [1 ]
机构
[1] ROCKEFELLER UNIV,NEW YORK,NY 10021
关键词
D O I
10.1126/science.8438166
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:1157 / 1161
页数:5
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