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