2ple
From Proteopedia
(New page: 200px<br /> <applet load="2ple" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ple" /> '''NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN ...) |
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'''NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE'''<br /> | '''NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PLE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with PO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 2PLE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=PO3:'>PO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: phosphoric diester hydrolase]] | [[Category: phosphoric diester hydrolase]] | ||
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Revision as of 15:41, 15 February 2008
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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
2PLE is a Protein complex structure of sequences from Bos taurus with as ligand. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 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
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