4cgv

From Proteopedia

(Difference between revisions)

Revision as of 10:26, 4 August 2016

First TPR of Spaghetti (RPAP3) bound to HSP90 peptide SRMEEVD

Structural highlights

4cgv is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4cgu, 4cgw, 4chh, 4ckt, 4cv4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RPAP3_HUMAN] Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.^[1] [HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.^[2] ^[3]

Publication Abstract from PubMed

Client protein recruitment to the Hsp90 system depends on cochaperones that bind the client and Hsp90 simultaneously and facilitate their interaction. Hsp90 involvement in the assembly of snoRNPs, RNA polymerases, PI3-kinase-like kinases, and chromatin remodeling complexes depends on the TTT (Tel2-Tti1-Tti2), and R2TP complexes-consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1 (Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)-that together provide the connection to Hsp90. The biochemistry underlying R2TP function is still poorly understood. Pih1 in particular, at the heart of the complex, has not been described at a structural level, nor have the multiple protein-protein interactions it mediates been characterized. Here we present a structural and biochemical analysis of Hsp90-Tah1-Pih1, Hsp90-Spagh, and Pih1D1-Tel2 complexes that reveal a domain in Pih1D1 specific for binding CK2 phosphorylation sites, and together define the structural basis by which the R2TP complex connects the Hsp90 chaperone system to the TTT complex.

Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1.,Pal M, Morgan M, Phelps SE, Roe SM, Parry-Morris S, Downs JA, Polier S, Pearl LH, Prodromou C Structure. 2014 Apr 30. pii: S0969-2126(14)00105-1. doi:, 10.1016/j.str.2014.04.001. PMID:24794838^[4]

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

References

↑ Jeronimo C, Forget D, Bouchard A, Li Q, Chua G, Poitras C, Therien C, Bergeron D, Bourassa S, Greenblatt J, Chabot B, Poirier GG, Hughes TR, Blanchette M, Price DH, Coulombe B. Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Mol Cell. 2007 Jul 20;27(2):262-74. PMID:17643375 doi:http://dx.doi.org/10.1016/j.molcel.2007.06.027
↑ Martinez-Ruiz A, Villanueva L, Gonzalez de Orduna C, Lopez-Ferrer D, Higueras MA, Tarin C, Rodriguez-Crespo I, Vazquez J, Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. Epub 2005 Jun 3. PMID:15937123 doi:10.1073/pnas.0407294102
↑ Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200
↑ Pal M, Morgan M, Phelps SE, Roe SM, Parry-Morris S, Downs JA, Polier S, Pearl LH, Prodromou C. Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1. Structure. 2014 Apr 30. pii: S0969-2126(14)00105-1. doi:, 10.1016/j.str.2014.04.001. PMID:24794838 doi:http://dx.doi.org/10.1016/j.str.2014.04.001

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cgv"

Categories: Pal, M | Roe, S M | Chaperone | Pih1 | R2tp | Tah1

@@ Line 1: / Line 1: @@
 ==First TPR of Spaghetti (RPAP3) bound to HSP90 peptide SRMEEVD==
 <StructureSection load='4cgv' size='340' side='right' caption='[[4cgv]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cgu|4cgu]], [[4cgw|4cgw]], [[4chh|4chh]], [[4ckt|4ckt]], [[4cv4|4cv4]]</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=4cgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cgv RCSB], [http://www.ebi.ac.uk/pdbsum/4cgv PDBsum]</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=4cgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cgv OCA], [http://pdbe.org/4cgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cgv RCSB], [http://www.ebi.ac.uk/pdbsum/4cgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cgv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4cgv" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4cgv

From Proteopedia

Revision as of 10:26, 4 August 2016

First TPR of Spaghetti (RPAP3) bound to HSP90 peptide SRMEEVD

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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