2d9d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2d9d" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:2d9d.png|left|200px]]
+
==Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5==
 +
<StructureSection load='2d9d' size='340' side='right' caption='[[2d9d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2d9d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D9D FirstGlance]. <br>
 +
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAG5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2d9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d9d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2d9d RCSB], [http://www.ebi.ac.uk/pdbsum/2d9d PDBsum], [http://www.topsan.org/Proteins/RSGI/2d9d TOPSAN]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
{{STRUCTURE_2d9d| PDB=2d9d | SCENE= }}
+
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<ref>PMID:20223214</ref>
-
===Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
-
{{ABSTRACT_PUBMED_20223214}}
+
==See Also==
-
 
+
*[[BAG protein|BAG protein]]
-
==About this Structure==
+
== References ==
-
[[2d9d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D9D OCA].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
<ref group="xtra">PMID:020223214</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Hatta, R.]]
[[Category: Hatta, R.]]

Revision as of 08:29, 8 October 2014

Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d9d"
Personal tools