Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain

被引:125
作者
Zhou, MM
Huang, BH
Olejniczak, ET
Meadows, RP
Shuker, SB
Miyazaki, M
Trub, T
Shoelson, SE
Fesik, SW
机构
[1] ABBOTT LABS,DIV PHARMACEUT DISCOVERY,ABBOTT PK,IL 60064
[2] HARVARD UNIV,SCH MED,JOSLIN DIABET CTR,BOSTON,MA 02215
[3] HARVARD UNIV,SCH MED,DEPT MED,BOSTON,MA 02215
来源
NATURE STRUCTURAL BIOLOGY | 1996年 / 3卷 / 04期
关键词
D O I
10.1038/nsb0496-388
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We present the NMR structure of the PTB domain of insulin receptor substrate-1 (IRS-1) complexed to a tyrosine-phosphorylated peptide derived from the IL-4 receptor. Despite the lack of sequence homology and different binding specificity, the overall fold of the protein is similar to that of the Shc PTB domain and closely resembles that of PH domains. However, the PTB domain of IRS-1 is smaller than that of Shc (110 Versus 170 residues) and binds to phosphopeptides in a distinct manner. We explain the phosphopeptide binding specificity based on the structure of the complex and results of site-directed mutagenesis experiments.
引用
收藏
页码:388 / 393
页数:6
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