1oo3
From Proteopedia
(New page: 200px<br /><applet load="1oo3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oo3" /> '''P395S mutant of the p85 regulatory subunit o...) |
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| - | [[Image:1oo3.gif|left|200px]]<br /><applet load="1oo3" size=" | + | [[Image:1oo3.gif|left|200px]]<br /><applet load="1oo3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oo3" /> | caption="1oo3" /> | ||
'''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase'''<br /> | '''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Understanding the specificity of Src homology 2 (SH2) domains is important | + | 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== | ==About this Structure== | ||
| - | 1OO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1OO3 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Guenther, U | + | [[Category: Guenther, U L.]] |
[[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:49 2008'' |
Revision as of 12:19, 21 February 2008
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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 Feb 21 14:19:49 2008
