2qw9

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[[Image:2qw9.jpg|left|200px]]
[[Image:2qw9.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2qw9 |SIZE=350|CAPTION= <scene name='initialview01'>2qw9</scene>, resolution 1.850&Aring;
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The line below this paragraph, containing "STRUCTURE_2qw9", creates the "Structure Box" on the page.
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|SITE=
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|GENE= HSPA8, HSC70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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|DOMAIN=
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{{STRUCTURE_2qw9| PDB=2qw9 | SCENE= }}
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|RELATEDENTRY=[[2qwl|2QWL]], [[2qwm|2QWM]], [[2qwn|2QWN]], [[2qwo|2QWO]], [[2qwp|2QWP]], [[2qwq|2QWQ]], [[2qwr|2QWR]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qw9 OCA], [http://www.ebi.ac.uk/pdbsum/2qw9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qw9 RCSB]</span>
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'''Crystal structure of bovine hsc70 (1-394aa)in the apo state'''
'''Crystal structure of bovine hsc70 (1-394aa)in the apo state'''
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[[Category: Taylor, A B.]]
[[Category: Taylor, A B.]]
[[Category: Wang, L.]]
[[Category: Wang, L.]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: cytoplasm]]
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[[Category: Cytoplasm]]
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[[Category: nucleotide-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: nucleus]]
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[[Category: Nucleus]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: stress response]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:48:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:54:01 2008''
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Revision as of 12:48, 4 May 2008

Image:2qw9.jpg

Template:STRUCTURE 2qw9

Crystal structure of bovine hsc70 (1-394aa)in the apo state


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.

About this Structure

2QW9 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 15:48:06 2008

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