1xqs: Difference between revisions

Revision as of 17:08, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xqs.png

Template:STRUCTURE 1xqs

Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domainCrystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domain

Template:ABSTRACT PUBMED 15694338

About this StructureAbout this Structure

1XQS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange., Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A, Mol Cell. 2005 Feb 4;17(3):367-79. PMID:15694338

Page seeded by OCA on Mon Jul 28 17:08:43 2008

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

OCA

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-'''Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domain'''
+===Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase domain===
-==Overview==
+<!--
-HspBP1 belongs to a family of eukaryotic proteins recently identified as nucleotide exchange factors for Hsp70. We show that the S. cerevisiae ortholog of HspBP1, Fes1p, is required for efficient protein folding in the cytosol at 37 degrees C. The crystal structure of HspBP1, alone and complexed with part of the Hsp70 ATPase domain, reveals a mechanism for its function distinct from that of BAG-1 or GrpE, previously characterized nucleotide exchange factors of Hsp70. HspBP1 has a curved, all alpha-helical fold containing four armadillo-like repeats unlike the other nucleotide exchange factors. The concave face of HspBP1 embraces lobe II of the ATPase domain, and a steric conflict displaces lobe I, reducing the affinity for nucleotide. In contrast, BAG-1 and GrpE trigger a conserved conformational change in lobe II of the ATPase domain. Thus, nucleotide exchange on eukaryotic Hsp70 occurs through two distinct mechanisms.
+The line below this paragraph, {{ABSTRACT_PUBMED_15694338}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15694338 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15694338}}
 ==About this Structure==
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 [[Category: Armadillo repeat]]
 [[Category: Superhelical twist]]
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