2qwp: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2qwp.jpg|left|200px]]
{{Seed}}
[[Image:2qwp.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qwp|  PDB=2qwp  |  SCENE=  }}  
{{STRUCTURE_2qwp|  PDB=2qwp  |  SCENE=  }}  


'''Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #2'''
===Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #2===




==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
(as it appears on PubMed at http://www.pubmed.gov), where 17996706 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17996706}}


==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Sh3-binding]]
[[Category: Sh3-binding]]
[[Category: Stress response]]
[[Category: Stress response]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:49:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:39:06 2008''

Revision as of 21:39, 27 July 2008

File:2qwp.png

Template:STRUCTURE 2qwp

Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #2

Template:ABSTRACT PUBMED 17996706

About this Structure

2QWP is a Protein complex structure of sequences 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 Mon Jul 28 00:39:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2qwp&oldid=673927"