Pascal S M, Singer A U, Gish G, Yamazaki T, Shoelson S E, Pawson T, Kay L E, Forman-Kay J D
Biochemistry Research Division, Hospital for Sick Children, Toronto, Ontario, Canada.
Cell. 1994 May 6;77(3):461-72. doi: 10.1016/0092-8674(94)90160-0.
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.
通过核磁共振光谱法，已确定了磷脂酶C-γ1（PLC-γ1）C端SH2结构域与对应于血小板衍生生长因子受体上其Tyr-1021高亲和力结合位点的磷酸肽形成的复合物的溶液结构。SH2-磷酸肽复合物的拓扑结构与先前报道的Src和Lck SH2复合物相似。然而，磷酸酪氨酸（pTyr）C端残基的结合位点是一个延伸的凹槽，它与相对于pTyr的+1至+6位的肽残基接触。与Src和Lck的这一显著差异反映了这样一个事实，即PLC-γ1复合物涉及与pTyr C端主要为疏水残基的磷酸肽结合，因此可作为第二类SH2-磷酸肽相互作用的原型。
