2qwr: Difference between revisions

Revision as of 06:04, 28 July 2008

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File:2qwr.png

Template:STRUCTURE 2qwr

Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP intact formCrystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP intact form

Template:ABSTRACT PUBMED 17996706

About this StructureAbout this Structure

2QWR is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of J cochaperone binding and regulation of Hsp70., Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R, Mol Cell. 2007 Nov 9;28(3):422-33. PMID:17996706

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP intact form'''
+===Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP intact form===
-==Overview==
+<!--
-The many protein processing reactions of the ATP-hydrolyzing Hsp70s are regulated by J cochaperones, which contain J domains that stimulate Hsp70 ATPase activity and accessory domains that present protein substrates to Hsp70s. We report the structure of a J domain complexed with a J responsive portion of a mammalian Hsp70. The J domain activates ATPase activity by directing the linker that connects the Hsp70 nucleotide binding domain (NBD) and substrate binding domain (SBD) toward a hydrophobic patch on the NBD surface. Binding of the J domain to Hsp70 displaces the SBD from the NBD, which may allow the SBD flexibility to capture diverse substrates. Unlike prokaryotic Hsp70, the SBD and NBD of the mammalian chaperone interact in the ADP state. Thus, although both nucleotides and J cochaperones modulate Hsp70 NBD:linker and NBD:SBD interactions, the intrinsic persistence of those interactions differs in different Hsp70s and this may optimize their activities for different cellular roles.
+The line below this paragraph, {{ABSTRACT_PUBMED_17996706}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17996706}}
 ==About this Structure==
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 [[Category: Sh3-binding]]
 [[Category: Stress response]]
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