2ple
From Proteopedia
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|PDB= 2ple |SIZE=350|CAPTION= <scene name='initialview01'>2ple</scene> | |PDB= 2ple |SIZE=350|CAPTION= <scene name='initialview01'>2ple</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=[[2pld|2PLD]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ple FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ple OCA], [http://www.ebi.ac.uk/pdbsum/2ple PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ple 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Myelomonocytic leukemia, chronic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173410 173410]], Myeloproliferative disorder with eosinophilia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173410 173410]] | ||
==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: PO3]] | ||
[[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 04:37:33 2008'' |
Revision as of 01:37, 31 March 2008
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| Ligands: | |||||||
| Activity: | Phosphoinositide phospholipase C, with EC number 3.1.4.11 | ||||||
| Related: | 2PLD
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE
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.
About this Structure
2PLE is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide., Pascal SM, Singer AU, Gish G, Yamazaki T, Shoelson SE, Pawson T, Kay LE, Forman-Kay JD, Cell. 1994 May 6;77(3):461-72. PMID:8181064
Page seeded by OCA on Mon Mar 31 04:37:33 2008
