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1uk5

From Proteopedia

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Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3

Structural highlights

1uk5 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

BAG3_MOUSE Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.

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

ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several cochaperones. BAG5 consists of five BAG domains and associates with the nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the cytosol reportedly disturbs Hsp70-mediated protein refolding and induces Parkinson's disease. In the present study, we found that the fifth BAG domain (BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also determined the crystal structures of the BD5*NBD complex. BD5 binding caused two different types of NBD conformational changes, which both disrupted the nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP. Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding.

The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.,Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S Structure. 2010 Mar 10;18(3):309-19. PMID:20223214^[1]

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

References

↑ Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S. The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure. 2010 Mar 10;18(3):309-19. PMID:20223214 doi:10.1016/j.str.2010.01.004

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uk5"

@@ Line 1: / Line 1: @@
 ==Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3==
-<StructureSection load='1uk5' size='340' side='right'caption='[[1uk5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1uk5' size='340' side='right'caption='[[1uk5]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1uk5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UK5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1UK5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1uk5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UK5 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FANTOM 2 cDNA 4931440G06 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1uk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uk5 OCA], [http://pdbe.org/1uk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uk5 RCSB], [http://www.ebi.ac.uk/pdbsum/1uk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uk5 ProSAT], [http://www.topsan.org/Proteins/RSGI/1uk5 TOPSAN]</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=1uk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uk5 OCA], [https://pdbe.org/1uk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uk5 RCSB], [https://www.ebi.ac.uk/pdbsum/1uk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uk5 ProSAT], [https://www.topsan.org/Proteins/RSGI/1uk5 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BAG3_MOUSE BAG3_MOUSE]] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.
+[https://www.uniprot.org/uniprot/BAG3_MOUSE BAG3_MOUSE] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Hatta, R]]
+[[Category: Hatta R]]
-[[Category: Hayashi, F]]
+[[Category: Hayashi F]]
-[[Category: Structural genomic]]
+[[Category: Yokoyama S]]
-[[Category: Yokoyama, S]]
+[[Category: Yoshida M]]
-[[Category: Yoshida, M]]
-[[Category: Bi]]
-[[Category: Cair-1]]
-[[Category: Chaperone]]
-[[Category: Rsgi]]
-[[Category: Triple helix bandle]]

1uk5

From Proteopedia

Current revision

Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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