View source for 6fdp


==NMR structure of the second TPR domain of the human RPAP3 protein in complex with HSP90 peptide DTSRMEEVD==
<StructureSection load='6fdp' size='340' side='right'caption='[[6fdp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fdp]] 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=6FDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FDP 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fdp OCA], [https://pdbe.org/6fdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fdp RCSB], [https://www.ebi.ac.uk/pdbsum/6fdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fdp ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
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<ref>PMID:30033218</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fdp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chagot ME]]
[[Category: Manival X]]
[[Category: Quinternet M]]