2PLE

NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE

2PLE の概要

• エントリーDOI: 10.2210/pdb2ple/pdb
• 分子名称: PHOSPHOLIPASE C GAMMA-1, C-TERMINAL SH2 DOMAIN, PHOSPHOPEPTIDE FROM PDGF (2 entities in total)
• 機能のキーワード: phosphoric diester hydrolase
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Cell projection, lamellipodium : P08487; Cell membrane; Single-pass type I membrane protein: P09619
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13756.46

構造登録者

Pascal, S.M.,Singer, A.U.,Gish, G.,Yamazaki, T.,Shoelson, S.E.,Pawson, T.,Kay, L.E.,Forman-Kay, J.D. (登録日: 1994-08-19, 公開日: 1995-01-26, 最終更新日: 2024-11-20)

主引用文献

Pascal, S.M.,Singer, A.U.,Gish, G.,Yamazaki, T.,Shoelson, S.E.,Pawson, T.,Kay, L.E.,Forman-Kay, J.D.
Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide.
Cell(Cambridge,Mass.), 77:461-472, 1994

PubMed Abstract: 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.

PubMed: 8181064
DOI: 10.1016/0092-8674(94)90160-0

実験手法

SOLUTION NMR