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1fu6
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fu5|1FU5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fu6 OCA], [http://www.ebi.ac.uk/pdbsum/1fu6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fu6 RCSB]</span> | ||
}} | }} | ||
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[[Category: central beta-sheet with two flanking alpha-helice]] | [[Category: central beta-sheet with two flanking alpha-helice]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:30:23 2008'' |
Revision as of 17:30, 30 March 2008
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| Related: | 1FU5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE
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
1FU6 is a Single protein structure of sequence 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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