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1fu5
From Proteopedia
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(New page: 200px<br /><applet load="1fu5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fu5" /> '''NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85...)
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Revision as of 13:10, 20 November 2007
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NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE COMPLEXED TO A DOUBLY PHOSPHORYLATED PEPTIDE DERIVED FROM POLYOMAVIRUS MIDDLE T ANTIGEN
Overview
The N-terminal src homology 2 (SH2) domain of the p85 subunit of, phosphoinositide 3-kinase (PI3K) has a higher affinity for a peptide with, two phosphotyrosines than for the same peptide with only one. This, unexpected result was not observed for the C-terminal SH2 from the same, protein. NMR structural analysis has been used to understand the behavior, of the N-SH2. The structure of the free SH2 domain has been compared to, that of the SH2 complexed with a doubly phosphorylated peptide derived, from polyomavirus middle T antigen (MT). The structure of the free SH2, domain shows some differences from previous NMR and X-ray structures. In, the N-SH2 complexed with a doubly phosphorylated peptide, a second site, for phosphotyrosine interaction has been identified. Further, line shapes, of NMR signals showed that the SH2 protein-ligand complex is subject to, temperature-dependent conformational mobility. Conformational mobility is, also supported by the spectra of the ligand peptide. A binding model which, accounts for these results is developed.
About this Structure
1FU5 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site., Weber T, Schaffhausen B, Liu Y, Gunther UL, Biochemistry. 2000 Dec 26;39(51):15860-9. PMID:11123912
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