journal cover

Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. II. Ligand-mediated activation of GRP94 molecular chaperone and peptide binding activity

The Journal of Biological Chemistry

May 19, 2000

J J WassenbergChristopher V Nicchitta

Abstract

The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol. Although this domain is essential for Hsp90 function, the molecular basis for adenosine n...read more

Mentioned in this Paper

Covalent Interaction
Heat-Shock Proteins 70
Adenosine
Quinones
Nucleotide Binding
HSP90AA1 gene
HSP90 Heat-Shock Proteins
Plasma Protein Binding Capacity
Lactones
Sequencing
13
Paper Details
References
  • References
  • Citations21
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations21
123

Similar Papers Found In These Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

Chaperones & Protein Folding

Chaperones are proteins that play an essential role in protein folding, stability, assembly, and degradation. Their depletion or dysfunction has been implicated in protein folding disorders. Here is the latest research.

© 2020 Meta ULC. All rights reserved

Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. II. Ligand-mediated activation of GRP94 molecular chaperone and peptide binding activity

The Journal of Biological Chemistry

May 19, 2000

J J WassenbergChristopher V Nicchitta

PMID: 10816560

DOI: 10.1074/jbc.m001476200

Abstract

The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket that also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol. Although this domain is essential for Hsp90 function, the molecular basis for adenosine n...read more

Mentioned in this Paper

Covalent Interaction
Heat-Shock Proteins 70
Adenosine
Quinones
Nucleotide Binding
HSP90AA1 gene
HSP90 Heat-Shock Proteins
Plasma Protein Binding Capacity
Lactones
Sequencing
13

Similar Papers Found In These Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

Chaperones & Protein Folding

Chaperones are proteins that play an essential role in protein folding, stability, assembly, and degradation. Their depletion or dysfunction has been implicated in protein folding disorders. Here is the latest research.

Related Papers

Paper Details
References
  • References
  • Citations21
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations21
123
/papers/ligand-interactions-in-the-adenosine-nucleotide-bi/10816560