2pld
From Proteopedia
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| - | [[Image:2pld.jpg|left|200px]] | + | [[Image:2pld.jpg|left|200px]] |
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| - | '''NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE''' | + | {{Structure |
| + | |PDB= 2pld |SIZE=350|CAPTION= <scene name='initialview01'>2pld</scene> | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PLD is a [ | + | 2PLD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLD OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8181064 8181064] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Phosphoinositide phospholipase C]] | [[Category: Phosphoinositide phospholipase C]] | ||
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[[Category: phosphoric diester hydrolase]] | [[Category: phosphoric diester hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:14:27 2008'' |
Revision as of 16:14, 20 March 2008
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| Ligands: | |||||||
| Activity: | Phosphoinositide phospholipase C, with EC number 3.1.4.11 | ||||||
| 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
Contents |
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.
Disease
Known diseases associated with this structure: Myelomonocytic leukemia, chronic OMIM:[173410], Myeloproliferative disorder with eosinophilia OMIM:[173410]
About this Structure
2PLD 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 Thu Mar 20 18:14:27 2008
