1pnj

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{{STRUCTURE_1pnj| PDB=1pnj | SCENE= }}
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==SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE==
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===SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE===
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<StructureSection load='1pnj' size='340' side='right' caption='[[1pnj]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_7684655}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pnj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PNJ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pni|2pni]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pnj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pnj RCSB], [http://www.ebi.ac.uk/pdbsum/1pnj PDBsum]</span></td></tr>
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<table>
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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/pn/1pnj_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/chain_selection.php?pdb_ID=2ata 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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SH3 domains are found in proteins associated with receptor tyrosine kinase signal transduction complexes. The solution structure of the SH3 domain of the 85 kd regulatory subunit of phosphatidylinositol 3-kinase is shown to be a compact beta barrel consisting of five beta strands arranged in two beta sheets of three and two strands. The structure is similar to that of chicken brain alpha spectrin but represents a distinct class of SH3 domain, with an insertion between the second and third beta strands that may influence binding specificity. 1H chemical shift changes induced by complex formation with a synthetic peptide derived from the SH3-binding protein dynamin, together with amino acid sequence comparisons, suggest that the ligand-binding site consists of a hydrophobic surface flanked by two charged loops.
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==About this Structure==
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Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase.,Booker GW, Gout I, Downing AK, Driscoll PC, Boyd J, Waterfield MD, Campbell ID Cell. 1993 May 21;73(4):813-22. PMID:7684655<ref>PMID:7684655</ref>
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[[1pnj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNJ OCA].
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==See Also==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Phsphatidylinositol 3-kinase|Phsphatidylinositol 3-kinase]]
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</div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:007684655</ref><references group="xtra"/>
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*[[Phosphoinositide 3-Kinases|Phosphoinositide 3-Kinases]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Booker, G W.]]
[[Category: Booker, G W.]]

Revision as of 04:27, 3 October 2014

SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE

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