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1oo4

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(New page: 200px<br /><applet load="1oo4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oo4" /> '''P395S mutant of the p85 regulatory subunit o...)
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[[Image:1oo4.gif|left|200px]]<br /><applet load="1oo4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oo4" />
 
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'''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase complexed to a peptide derived from PDGFr'''<br />
 
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==Overview==
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==P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase complexed to a peptide derived from PDGFr==
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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.
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<StructureSection load='1oo4' size='340' side='right'caption='[[1oo4]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oo4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OO4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oo4 OCA], [https://pdbe.org/1oo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oo4 RCSB], [https://www.ebi.ac.uk/pdbsum/1oo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oo4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/P85A_BOVIN P85A_BOVIN] Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oo/1oo4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oo4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:14503862</ref>
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1OO4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OO4 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14503862 14503862]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1oo4" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Guenther, U.L.]]
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[[Category: Schaffhausen, B.]]
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[[Category: Weyrauch, B.]]
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[[Category: pdgfr complex]]
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[[Category: src homology 2 domain p85 regulatory subunit mutant]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:03:26 2007''
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==See Also==
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*[[Phosphoinositide 3-kinase 3D structures|Phosphoinositide 3-kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Guenther UL]]
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[[Category: Schaffhausen B]]
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[[Category: Weyrauch B]]

Current revision

P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase complexed to a peptide derived from PDGFr

PDB ID 1oo4

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