1qja: Difference between revisions
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New page: left|200px<br /> <applet load="1qja" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qja, resolution 2.0Å" /> '''14-3-3 ZETA/PHOSPHOP... |
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== | ==14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)== | ||
We have solved the high-resolution X-ray structure of 14-3-3 bound to two | <StructureSection load='1qja' size='340' side='right'caption='[[1qja]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== Function == | |||
[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> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/1qja_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1qja" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[14-3-3 protein|14-3-3 protein]] | |||
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Budman | [[Category: Budman J]] | ||
[[Category: Cantley | [[Category: Cantley LC]] | ||
[[Category: Gamblin | [[Category: Gamblin SJ]] | ||
[[Category: Rittinger | [[Category: Rittinger K]] | ||
[[Category: Smerdon | [[Category: Smerdon SJ]] | ||
[[Category: Volinia | [[Category: Volinia S]] | ||
[[Category: Xu | [[Category: Xu J]] | ||
[[Category: Yaffe | [[Category: Yaffe MB]] | ||
Latest revision as of 04:50, 17 October 2024
14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2)
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