2pld: Difference between revisions

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==Overview==

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.

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.

==Disease==

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[[Category: Phosphoinositide phospholipase C]]

[[Category: Protein complex]]

[[Category: Forman-Kay, J.D.]]

[[Category: Forman-Kay, J D.]]

[[Category: Gish, G.]]

[[Category: Kay, L.E.]]

[[Category: Kay, L E.]]

[[Category: Pascal, S.M.]]

[[Category: Pascal, S M.]]

[[Category: Pawson, T.]]

[[Category: Shoelson, S.E.]]

[[Category: Shoelson, S E.]]

[[Category: Singer, A.U.]]

[[Category: Singer, A U.]]

[[Category: Yamazaki, T.]]

[[Category: PO3]]

[[Category: phosphoric diester hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 17~~:41:41 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:44 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Phosphoinositide phospholipase C]]
 [[Category: Protein complex]]
-[[Category: Forman-Kay, J.D.]]
+[[Category: Forman-Kay, J D.]]
 [[Category: Gish, G.]]
-[[Category: Kay, L.E.]]
+[[Category: Kay, L E.]]
-[[Category: Pascal, S.M.]]
+[[Category: Pascal, S M.]]
 [[Category: Pawson, T.]]
-[[Category: Shoelson, S.E.]]
+[[Category: Shoelson, S E.]]
-[[Category: Singer, A.U.]]
+[[Category: Singer, A U.]]
 [[Category: Yamazaki, T.]]
 [[Category: PO3]]
 [[Category: phosphoric diester hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:41:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:44 2008''