6ez4

From Proteopedia

(Difference between revisions)

Revision as of 08:13, 14 June 2018

NMR structure of the C-terminal domain of the human RPAP3 protein

Structural highlights

6ez4 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	RPAP3 (HUMAN)
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

R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-alpha2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-alpha2 expression and for the assembly of liprin-alpha2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 degrees C, suggesting that R2SP could help compensating the lower temperate of testis.

The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.,Maurizy C, Quinternet M, Abel Y, Verheggen C, Santo PE, Bourguet M, C F Paiva A, Bragantini B, Chagot ME, Robert MC, Abeza C, Fabre P, Fort P, Vandermoere F, M F Sousa P, Rain JC, Charpentier B, Cianferani S, Bandeiras TM, Pradet-Balade B, Manival X, Bertrand E Nat Commun. 2018 May 29;9(1):2093. doi: 10.1038/s41467-018-04431-1. PMID:29844425^[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
↑ Maurizy C, Quinternet M, Abel Y, Verheggen C, Santo PE, Bourguet M, C F Paiva A, Bragantini B, Chagot ME, Robert MC, Abeza C, Fabre P, Fort P, Vandermoere F, M F Sousa P, Rain JC, Charpentier B, Cianferani S, Bandeiras TM, Pradet-Balade B, Manival X, Bertrand E. The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones. Nat Commun. 2018 May 29;9(1):2093. doi: 10.1038/s41467-018-04431-1. PMID:29844425 doi:http://dx.doi.org/10.1038/s41467-018-04431-1

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/6ez4"

@@ Line 3: / Line 3: @@
 <StructureSection load='6ez4' size='340' side='right' caption='[[6ez4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ez4]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EZ4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ez4]] is a 1 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=6EZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EZ4 FirstGlance]. <br>
-</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=6ez4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ez4 OCA], [http://pdbe.org/6ez4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ez4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ez4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ez4 ProSAT]</span></td></tr>
+</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])</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=6ez4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ez4 OCA], [http://pdbe.org/6ez4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ez4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ez4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ez4 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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-alpha2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-alpha2 expression and for the assembly of liprin-alpha2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 degrees C, suggesting that R2SP could help compensating the lower temperate of testis.
+The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones.,Maurizy C, Quinternet M, Abel Y, Verheggen C, Santo PE, Bourguet M, C F Paiva A, Bragantini B, Chagot ME, Robert MC, Abeza C, Fabre P, Fort P, Vandermoere F, M F Sousa P, Rain JC, Charpentier B, Cianferani S, Bandeiras TM, Pradet-Balade B, Manival X, Bertrand E Nat Commun. 2018 May 29;9(1):2093. doi: 10.1038/s41467-018-04431-1. PMID:29844425<ref>PMID:29844425</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6ez4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Bragantini, B]]
 [[Category: Chagot, M E]]

6ez4

From Proteopedia

Revision as of 08:13, 14 June 2018

NMR structure of the C-terminal domain of the human RPAP3 protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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