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6fdt

From Proteopedia

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Current revision

NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP70 peptide SGPTIEEVD

Structural highlights

6fdt 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.
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]

Publication Abstract from PubMed

RPAP3 and PIH1D1 are part of the HSP90 co-chaperone R2TP complex involved in the assembly process of many molecular machines. In this study, we performed a deep structural investigation of the HSP binding abilities of the two TPR domains of RPAP3. We combined 3D NMR, non-denaturing MS, and ITC techniques with Y2H, IP-LUMIER, FRET, and ATPase activity assays and explain the fundamental role played by the second TPR domain of RPAP3 in the specific recruitment of HSP90. We also established the 3D structure of an RPAP3:PIH1D1 sub-complex demonstrating the need for a 34-residue insertion, specific of RPAP3 isoform 1, for the tight binding of PIH1D1. We also confirm the existence of a complex lacking PIH1D1 in human cells (R2T), which shows differential binding to certain clients. These results highlight similarities and differences between the yeast and human R2TP complexes, and document the diversification of this family of co-chaperone complexes in human.

Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex.,Henri J, Chagot ME, Bourguet M, Abel Y, Terral G, Maurizy C, Aigueperse C, Georgescauld F, Vandermoere F, Saint-Fort R, Behm-Ansmant I, Charpentier B, Pradet-Balade B, Verheggen C, Bertrand E, Meyer P, Cianferani S, Manival X, Quinternet M Structure. 2018 Jul 18. pii: S0969-2126(18)30208-9. doi:, 10.1016/j.str.2018.06.002. PMID:30033218^[2]

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
↑ Henri J, Chagot ME, Bourguet M, Abel Y, Terral G, Maurizy C, Aigueperse C, Georgescauld F, Vandermoere F, Saint-Fort R, Behm-Ansmant I, Charpentier B, Pradet-Balade B, Verheggen C, Bertrand E, Meyer P, Cianferani S, Manival X, Quinternet M. Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex. Structure. 2018 Jul 18. pii: S0969-2126(18)30208-9. doi:, 10.1016/j.str.2018.06.002. PMID:30033218 doi:http://dx.doi.org/10.1016/j.str.2018.06.002

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/6fdt"

Categories: Homo sapiens | Large Structures | Chagot ME | Manival X | Quinternet M

@@ Line 1: / Line 1: @@
 ==NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP70 peptide SGPTIEEVD==
-<StructureSection load='6fdt' size='340' side='right' caption='[[6fdt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6fdt' size='340' side='right'caption='[[6fdt]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6fdt]] 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=6FDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FDT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6fdt]] 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=6FDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FDT FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPAP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HSPA1B, HSP72 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=6fdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fdt OCA], [https://pdbe.org/6fdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fdt RCSB], [https://www.ebi.ac.uk/pdbsum/6fdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fdt 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=6fdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fdt OCA], [http://pdbe.org/6fdt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fdt RCSB], [http://www.ebi.ac.uk/pdbsum/6fdt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fdt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RPAP3_HUMAN 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.<ref>PMID:17643375</ref>  [[http://www.uniprot.org/uniprot/HS71B_HUMAN HS71B_HUMAN]] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:23973223</ref>
+[https://www.uniprot.org/uniprot/RPAP3_HUMAN 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.<ref>PMID:17643375</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Chagot, M E]]
+[[Category: Large Structures]]
-[[Category: Manival, X]]
+[[Category: Chagot ME]]
-[[Category: Quinternet, M]]
+[[Category: Manival X]]
-[[Category: Chaperone]]
+[[Category: Quinternet M]]
-[[Category: Tpr hsp ruvbl polymerase]]

6fdt

From Proteopedia

Current revision

NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP70 peptide SGPTIEEVD

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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