This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1oo3
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1oo3.gif|left|200px]] | [[Image:1oo3.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1oo3", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1oo3| PDB=1oo3 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''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''' | ||
| Line 28: | Line 25: | ||
[[Category: Schaffhausen, B.]] | [[Category: Schaffhausen, B.]] | ||
[[Category: Weyrauch, B.]] | [[Category: Weyrauch, B.]] | ||
| - | [[Category: | + | [[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 | + | |
Revision as of 01:05, 3 May 2008
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 Sat May 3 04:05:24 2008
