SOLUTION STRUCTURE OF THE SH3 DOMAIN OF SRC AND IDENTIFICATION OF ITS LIGAND-BINDING SITE

被引:304
|
作者
YU, HT
ROSEN, MK
SHIN, TB
SEIDELDUGAN, C
BRUGGE, JS
SCHREIBER, SL
机构
[1] HARVARD UNIV,DEPT CHEM,CAMBRIDGE,MA 02138
[2] ARIAD PHARMACEUT INC,CAMBRIDGE,MA 02139
关键词
D O I
10.1126/science.1280858
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 protein domain of 55 to 75 amino acids found in many cytoplasmic proteins, including those that participate in signal transduction pathways. The solution structure of the SH3 domain of the tyrosine kinase Src was determined by multidimensional nuclear magnetic resonance methods. The molecule is composed of two short three-stranded anti-parallel beta sheets packed together at approximately right angles. Studies of the SH3 domain bound to proline-rich peptide ligands revealed a hydrophobic binding site on the surface of the protein that is lined with the side chains of conserved aromatic amino acids.
引用
收藏
页码:1665 / 1668
页数:4
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