1fu5: Difference between revisions

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[[Image:1fu5.gif|left|200px]]
[[Image:1fu5.gif|left|200px]]


{{Structure
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{{STRUCTURE_1fu5| PDB=1fu5  | SCENE= }}  
|RELATEDENTRY=[[1fu6|1FU6]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fu5 OCA], [http://www.ebi.ac.uk/pdbsum/1fu5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fu5 RCSB]</span>
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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'''
'''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'''
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[[Category: Schaffhausen, B.]]
[[Category: Schaffhausen, B.]]
[[Category: Weber, T.]]
[[Category: Weber, T.]]
[[Category: protein-peptide complex]]
[[Category: Protein-peptide complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:46:13 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:30:22 2008''

Revision as of 16:46, 2 May 2008

File:1fu5.gif

Template:STRUCTURE 1fu5

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


OverviewOverview

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 StructureAbout this Structure

1FU5 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 16:46:13 2008

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