1qja

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[[Image:1qja.jpg|left|200px]]
 
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{{Structure
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==14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)==
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|PDB= 1qja |SIZE=350|CAPTION= <scene name='initialview01'>1qja</scene>, resolution 2.0&Aring;
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<StructureSection load='1qja' size='340' side='right'caption='[[1qja]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>
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<table><tr><td colspan='2'>[[1qja]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJA FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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|DOMAIN=
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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=1qja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qja OCA], [https://pdbe.org/1qja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qja RCSB], [https://www.ebi.ac.uk/pdbsum/1qja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qja ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qja OCA], [http://www.ebi.ac.uk/pdbsum/1qja PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qja RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref>
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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/qj/1qja_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1qja 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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We have solved the high-resolution X-ray structure of 14-3-3 bound to two different phosphoserine peptides, representing alternative substrate-binding motifs. These structures reveal an evolutionarily conserved network of peptide-protein interactions within all 14-3-3 isotypes, explain both binding motifs, and identify a novel intrachain phosphorylation-mediated loop structure in one of the peptides. A 14-3-3 mutation disrupting Raf signaling alters the ligand-binding cleft, selecting a different phosphopeptide-binding motif and different substrates than the wild-type protein. Many 14-3-3: peptide contacts involve a C-terminal amphipathic alpha helix containing a putative nuclear export signal, implicating this segment in both ligand and Crm1 binding. Structural homology between the 14-3-3 NES structure and those within I kappa B alpha and p53 reveals a conserved topology recognized by the Crm1 nuclear export machinery.
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'''14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)'''
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Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding.,Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB Mol Cell. 1999 Aug;4(2):153-66. PMID:10488331<ref>PMID:10488331</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1qja" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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We have solved the high-resolution X-ray structure of 14-3-3 bound to two different phosphoserine peptides, representing alternative substrate-binding motifs. These structures reveal an evolutionarily conserved network of peptide-protein interactions within all 14-3-3 isotypes, explain both binding motifs, and identify a novel intrachain phosphorylation-mediated loop structure in one of the peptides. A 14-3-3 mutation disrupting Raf signaling alters the ligand-binding cleft, selecting a different phosphopeptide-binding motif and different substrates than the wild-type protein. Many 14-3-3: peptide contacts involve a C-terminal amphipathic alpha helix containing a putative nuclear export signal, implicating this segment in both ligand and Crm1 binding. Structural homology between the 14-3-3 NES structure and those within I kappa B alpha and p53 reveals a conserved topology recognized by the Crm1 nuclear export machinery.
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*[[14-3-3 protein|14-3-3 protein]]
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*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
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==About this Structure==
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== References ==
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1QJA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJA OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding., Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB, Mol Cell. 1999 Aug;4(2):153-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10488331 10488331]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Budman, J.]]
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[[Category: Budman J]]
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[[Category: Cantley, L C.]]
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[[Category: Cantley LC]]
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[[Category: Gamblin, S J.]]
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[[Category: Gamblin SJ]]
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[[Category: Rittinger, K.]]
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[[Category: Rittinger K]]
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[[Category: Smerdon, S J.]]
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[[Category: Smerdon SJ]]
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[[Category: Volinia, S.]]
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[[Category: Volinia S]]
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[[Category: Xu, J.]]
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[[Category: Xu J]]
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[[Category: Yaffe, M B.]]
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[[Category: Yaffe MB]]
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[[Category: 14-3-3]]
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[[Category: complex]]
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[[Category: phosphopeptide]]
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[[Category: signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:14:25 2008''
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Current revision

14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)

PDB ID 1qja

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