Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change (Q42659468)

4 November 2017

Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change (English)

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4 November 2017

endoplasmic reticulum

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author name string

D Eric Dollins

series ordinal

1

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4 November 2017

Robert M Immormino

series ordinal

2

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4 November 2017

Daniel T Gewirth

series ordinal

3

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4 November 2017

language of work or name

English

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publication date

11 June 2005

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Journal of Biological Chemistry

4 November 2017

10

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based on heuristic

inferred from page(s)

published in

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280

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34

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30438-30447

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Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability

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Leishmania LPG3 encodes a GRP94 homolog required for phosphoglycan synthesis implicated in parasite virulence but not viability

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Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway

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The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase

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Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

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Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells

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Hsp90-mediated folding of the lymphoid cell kinase p56lck

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

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Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair

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Crystal structure of an N-terminal fragment of the DNA gyrase B protein.

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GHKL, an emergent ATPase/kinase superfamily

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The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

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Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform

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Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone

21 January 2018

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Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation

21 January 2018

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Processing of X-ray diffraction data collected in oscillation mode

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Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Structure validation by Calpha geometry: phi,psi and Cbeta deviation

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New tools and data for improving structures, using all-atom contacts

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Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding

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N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle

21 January 2018

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Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

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Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

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21 January 2018

Identifiers

DOI

10.1074/JBC.M503761200

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4 November 2017

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