2PLE

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

Summary for 2PLE

• Entry DOI: 10.2210/pdb2ple/pdb
• Descriptor: PHOSPHOLIPASE C GAMMA-1, C-TERMINAL SH2 DOMAIN, PHOSPHOPEPTIDE FROM PDGF (2 entities in total)
• Functional Keywords: phosphoric diester hydrolase
• Biological source: Bos taurus (cattle); More
• Cellular location: Cell projection, lamellipodium : P08487; Cell membrane; Single-pass type I membrane protein: P09619
• Total number of polymer chains: 2
• Total formula weight: 13756.46

Authors

Pascal, S.M.,Singer, A.U.,Gish, G.,Yamazaki, T.,Shoelson, S.E.,Pawson, T.,Kay, L.E.,Forman-Kay, J.D. (deposition date: 1994-08-19, release date: 1995-01-26, Last modification date: 2017-11-29)

Primary citation

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

Experimental method

SOLUTION NMR