2pld: Difference between revisions
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|PDB= 2pld |SIZE=350|CAPTION= <scene name='initialview01'>2pld</scene> | |PDB= 2pld |SIZE=350|CAPTION= <scene name='initialview01'>2pld</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PO3:PHOSPHITE ION'>PO3</scene> | |LIGAND= <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ple|2PLE]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pld OCA], [http://www.ebi.ac.uk/pdbsum/2pld PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pld RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Singer, A U.]] | [[Category: Singer, A U.]] | ||
[[Category: Yamazaki, T.]] | [[Category: Yamazaki, T.]] | ||
[[Category: phosphoric diester hydrolase]] | [[Category: phosphoric diester hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:37:31 2008'' | ||
