1tc6: Difference between revisions

Revision as of 17:03, 27 July 2008

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File:1tc6.png

Template:STRUCTURE 1tc6

Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-ComplexLigand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex

Template:ABSTRACT PUBMED 15292259

About this StructureAbout this Structure

1TC6 is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

ReferenceReference

Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone., Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT, J Biol Chem. 2004 Oct 29;279(44):46162-71. Epub 2004 Aug 2. PMID:15292259

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-'''Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex'''
+===Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex===
-==Overview==
+<!--
-GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_15292259}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15292259 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15292259}}
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 [[Category: Grp94]]
 [[Category: Hsp90]]
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