1oo3: Difference between revisions

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[[Image:1oo3.gif|left|200px]]
[[Image:1oo3.gif|left|200px]]


{{Structure
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{{STRUCTURE_1oo3| PDB=1oo3  | SCENE= }}  
|RELATEDENTRY=[[1oo4|1OO4]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oo3 OCA], [http://www.ebi.ac.uk/pdbsum/1oo3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oo3 RCSB]</span>
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'''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase'''
'''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase'''
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[[Category: Schaffhausen, B.]]
[[Category: Schaffhausen, B.]]
[[Category: Weyrauch, B.]]
[[Category: Weyrauch, B.]]
[[Category: src homology 2 domain p85 regulatory subunit mutant]]
[[Category: Src homology 2 domain p85 regulatory subunit mutant]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:05:24 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:06 2008''

Revision as of 04:05, 3 May 2008

File:1oo3.gif

Template:STRUCTURE 1oo3

P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase


OverviewOverview

Understanding the specificity of Src homology 2 (SH2) domains is important because of their critical role in cell signaling. Previous genetic analysis has characterized mutants of the N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K). The P395S mutant exhibits a specificity for phosphopeptide binding different from that of the wild-type SH2. The P395S mutant has an increased affinity for the platelet-derived growth factor receptor (PDGFr) compared to polyomavirus middle T antigen (MT). Solution structures of the P395S mutant of the p85 N-SH2 alone and complexed to a PDGFr phosphopeptide were determined to explain the change in specificity. Chemical shift perturbations caused by different peptides were compared for mutant and wild-type structures. The results show that the single P395S mutation has broad effects on the structure. Furthermore, they provide a rationale for the observed changes in binding preference.

About this StructureAbout this Structure

1OO3 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Nuclear magnetic resonance structure of the P395S mutant of the N-SH2 domain of the p85 subunit of PI3 kinase: an SH2 domain with altered specificity., Gunther UL, Weyrauch B, Zhang X, Schaffhausen B, Biochemistry. 2003 Sep 30;42(38):11120-7. PMID:14503862 Page seeded by OCA on Sat May 3 04:05:24 2008

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