1oo3
From Proteopedia
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| - | [[Image:1oo3.gif|left|200px]] | + | [[Image:1oo3.gif|left|200px]] |
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| - | '''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase''' | + | {{Structure |
| + | |PDB= 1oo3 |SIZE=350|CAPTION= <scene name='initialview01'>1oo3</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OO3 is a [ | + | 1OO3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO3 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14503862 14503862] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:13:24 2008'' |
Revision as of 11:13, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase
Overview
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 Structure
1OO3 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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 Thu Mar 20 13:13:24 2008
