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3d0t

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Revision as of 10:58, 25 December 2014

Structure of the BNB domain of the Hsp70 cochaperone Bag2

Structural highlights

3d0t is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3cqx
Gene:	Bag2 (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[BAG2_MOUSE] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity).

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

Cochaperones are essential for Hsp70- and Hsc70-mediated folding of proteins and include nucleotide-exchange factors (NEFs) that assist protein folding by accelerating ADP-ATP exchange on Hsp70. The cochaperone Bag2 binds misfolded Hsp70 clients and also acts as an NEF, but the molecular basis for its function is unclear. We show that, rather than being a member of the Bag domain family, Bag2 contains a new type of Hsp70 NEF domain, which we call the 'brand new bag' (BNB) domain. Free and Hsc70-bound crystal structures of Bag2-BNB show its dimeric structure, in which a flanking linker helix and loop bind to Hsc70 to promote nucleotide exchange. NMR analysis demonstrates that the client binding sites and Hsc70-interaction sites of the Bag2-BNB overlap, and that Hsc70 can displace clients from Bag2-BNB, indicating a distinct mechanism for the regulation of Hsp70-mediated protein folding by Bag2.

Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2.,Xu Z, Page RC, Gomes MM, Kohli E, Nix JC, Herr AB, Patterson C, Misra S Nat Struct Mol Biol. 2008 Dec;15(12):1309-17. Epub 2008 Nov 23. PMID:19029896^[1]

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

References

↑ Xu Z, Page RC, Gomes MM, Kohli E, Nix JC, Herr AB, Patterson C, Misra S. Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2. Nat Struct Mol Biol. 2008 Dec;15(12):1309-17. Epub 2008 Nov 23. PMID:19029896 doi:10.1038/nsmb.1518

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3d0t"

@@ Line 7: / Line 7: @@
 <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=3d0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d0t RCSB], [http://www.ebi.ac.uk/pdbsum/3d0t PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/BAG2_MOUSE BAG2_MOUSE]] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 </StructureSection>
 [[Category: Mus musculus]]
-[[Category: Devlin, K.]]
+[[Category: Devlin, K]]
-[[Category: Misra, S.]]
+[[Category: Misra, S]]
-[[Category: Nix, J C.]]
+[[Category: Nix, J C]]
-[[Category: Xu, Z.]]
+[[Category: Xu, Z]]
 [[Category: 4-helix bundle]]
 [[Category: Chaperone]]

3d0t

From Proteopedia

Revision as of 10:58, 25 December 2014

Structure of the BNB domain of the Hsp70 cochaperone Bag2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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