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2bug

From Proteopedia

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Current revision

Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide

Structural highlights

2bug is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cliff MJ, Harris R, Barford D, Ladbury JE, Williams MA. Conformational diversity in the TPR domain-mediated interaction of protein phosphatase 5 with Hsp90. Structure. 2006 Mar;14(3):415-26. PMID:16531226 doi:10.1016/j.str.2005.12.009

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bug"

@@ Line 1: / Line 1: @@
 ==Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide==
-<StructureSection load='2bug' size='340' side='right' caption='[[2bug]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
+<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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BUG FirstGlance]. <br>
+<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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a17|1a17]], [[1s95|1s95]], [[1wao|1wao]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bug OCA], [http://pdbe.org/2bug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bug RCSB], [http://www.ebi.ac.uk/pdbsum/2bug PDBsum], [http://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]]
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Serine/threonine protein phosphatase|Serine/threonine protein phosphatase]]
+*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Large Structures]]
-[[Category: Barford, D]]
+[[Category: Barford D]]
-[[Category: Cliff, M J]]
+[[Category: Cliff MJ]]
-[[Category: Harris, R]]
+[[Category: Harris R]]
-[[Category: Ladbury, J E]]
+[[Category: Ladbury JE]]
-[[Category: Williams, M A]]
+[[Category: Williams MA]]
-[[Category: Hsp90 binding]]
-[[Category: Hydrolase]]
-[[Category: Iron]]
-[[Category: Manganese]]
-[[Category: Metal-binding]]
-[[Category: Protein phosphatase]]
-[[Category: Tetratricopeptide domain]]

2bug

From Proteopedia

Current revision

Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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