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New page: left|200px<br /> <applet load="2bug" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bug" /> '''SOLUTION STRUCTURE OF THE TPR DOMAIN FROM P... |
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== | ==Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide== | ||
Protein phosphatase 5 (Ppp5) is one of several proteins that bind to the | <StructureSection load='2bug' size='340' side='right'caption='[[2bug]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bug]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=2bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bug OCA], [https://pdbe.org/2bug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bug RCSB], [https://www.ebi.ac.uk/pdbsum/2bug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bug ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PPP5_HUMAN PPP5_HUMAN] May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1. | |||
== 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/bu/2bug_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2bug ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein phosphatase 5 (Ppp5) is one of several proteins that bind to the Hsp90 chaperone via a tetratricopeptide repeat (TPR) domain. We report the solution structure of a complex of the TPR domain of Ppp5 with the C-terminal pentapeptide of Hsp90. This structure has the "two-carboxylate clamp" mechanism of peptide binding first seen in the Hop-TPR domain complexes with Hsp90 and Hsp70 peptides. However, NMR data reveal that the Ppp5 clamp is highly dynamic, and that there are multiple modes of peptide binding and mobility throughout the complex. Although this interaction is of very high affinity, relatively few persistent contacts are found between the peptide and the Ppp5-TPR domain, thus explaining its promiscuity in binding both Hsp70 and Hsp90 in vivo. We consider the possible implications of this dynamic structure for the mechanism of relief of autoinhibition in Ppp5 and for the mechanisms of TPR-mediated recognition of Hsp90 by other proteins. | |||
Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90.,Cliff MJ, Harris R, Barford D, Ladbury JE, Williams MA Structure. 2006 Mar;14(3):415-26. PMID:16531226<ref>PMID:16531226</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bug" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Barford D]] | |||
[[Category: Barford | [[Category: Cliff MJ]] | ||
[[Category: Cliff | [[Category: Harris R]] | ||
[[Category: Harris | [[Category: Ladbury JE]] | ||
[[Category: Ladbury | [[Category: Williams MA]] | ||
[[Category: Williams | |||
Latest revision as of 14:23, 22 May 2024
Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptideSolution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide
Structural highlights
FunctionPPP5_HUMAN May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein phosphatase 5 (Ppp5) is one of several proteins that bind to the Hsp90 chaperone via a tetratricopeptide repeat (TPR) domain. We report the solution structure of a complex of the TPR domain of Ppp5 with the C-terminal pentapeptide of Hsp90. This structure has the "two-carboxylate clamp" mechanism of peptide binding first seen in the Hop-TPR domain complexes with Hsp90 and Hsp70 peptides. However, NMR data reveal that the Ppp5 clamp is highly dynamic, and that there are multiple modes of peptide binding and mobility throughout the complex. Although this interaction is of very high affinity, relatively few persistent contacts are found between the peptide and the Ppp5-TPR domain, thus explaining its promiscuity in binding both Hsp70 and Hsp90 in vivo. We consider the possible implications of this dynamic structure for the mechanism of relief of autoinhibition in Ppp5 and for the mechanisms of TPR-mediated recognition of Hsp90 by other proteins. Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90.,Cliff MJ, Harris R, Barford D, Ladbury JE, Williams MA Structure. 2006 Mar;14(3):415-26. PMID:16531226[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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