NUCLEAR-MAGNETIC-RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA-1 COMPLEXED WITH A HIGH-AFFINITY BINDING PEPTIDE

被引：235
作者：
PASCAL, SM
SINGER, AU
GISH, G
YAMAZAKI, T
SHOELSON, SE
PAWSON, T
KAY, LE
FORMANKAY, JD
机构：
[1] MT SINAI HOSP, SAMUEL LUNENFELD RES INST, DIV MOLEC & DEV BIOL, TORONTO M5G 1X5, ON, CANADA
[2] UNIV TORONTO, PROT ENGN NETWORK CTR EXCELLENCE, TORONTO M5S 1A8, ON, CANADA
[3] UNIV TORONTO, DEPT MED GENET, TORONTO M5S 1A8, ON, CANADA
[4] UNIV TORONTO, DEPT BIOCHEM, TORONTO M5S 1A8, ON, CANADA
[5] UNIV TORONTO, DEPT CHEM, TORONTO M5S 1A8, ON, CANADA
[6] BRIGHAM & WOMENS HOSP, JOSLIN DIABET CTR, BOSTON, MA 02215 USA
[7] BRIGHAM & WOMENS HOSP, DEPT MED, BOSTON, MA 02215 USA
[8] HARVARD UNIV, SCH MED, BOSTON, MA 02215 USA
来源：
CELL | 1994年 / 77卷 / 03期
基金：
英国医学研究理事会;
关键词：
D O I：
10.1016/0092-8674(94)90160-0
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：
The solution structure of the C-terminal SH2 domain of phospholipase C-gamma 1 (PLC-gamma 1), in complex with a phosphopeptide corresponding to its Tyr-1021 high affinity binding site on the platelet-derived growth factor receptor, has been determined by nuclear magnetic resonance spectroscopy. The topology of the SH2-phosphopeptide complex is similar to previously reported Src and Lck SH2 complexes. However, the binding site for residues C-terminal to the phosphotyrosine (pTyr) is an extended groove that contacts peptide residues at the +1 to +6 positions relative to the pTyr. This striking difference from Src and Lck reflects the fact that the PLC-gamma 1 complex involves binding of a phosphopeptide with predominantly hydrophobic residues C-terminal to the pTyr and therefore serves as a prototype for a second class of SH2-phosphopeptide interactions.
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收藏
页码：461 / 472
页数：12
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