1tc0

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{{STRUCTURE_1tc0| PDB=1tc0 | SCENE= }}
{{STRUCTURE_1tc0| PDB=1tc0 | SCENE= }}
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'''Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP'''
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===Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15292259 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15292259}}
==About this Structure==
==About this Structure==
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[[Category: Grp94]]
[[Category: Grp94]]
[[Category: Hsp90]]
[[Category: Hsp90]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:46:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:58:33 2008''

Revision as of 09:58, 27 July 2008

Template:STRUCTURE 1tc0

Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP

Template:ABSTRACT PUBMED 15292259

About this Structure

1TC0 is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.

Reference

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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