Journal article
Identification of the N-terminal Peptide Binding Site of Glucose-regulated Protein 94
The Journal of biological chemistry, v 279(16), pp 16543-16552
16 Apr 2004
PMID: 14754890
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Because the stress protein GRP94 can augment presentation of peptides to T cells, it is important to define how it, as well as all other HSP90 family members, binds peptides. Having previously shown that the N-terminal half of GRP94 can account for the peptide binding activity of the full-length protein, we now locate this binding site by testing predictions of a molecular docking model. The best predicted site was on the opposite face of the β sheet from the pan-HSP90 radicicol-binding pocket, in close proximity to a deep hydrophobic pocket. The peptide and radicicol-binding sites are distinct, as shown by the ability of a radicicol-refractive mutant to bind peptide. When the fluorophore acrylodan is attached to Cys117 within the hydrophobic pocket, its fluorescence is reduced upon peptide binding, consistent with proximity of the two ligands. Substitution of His125, which contacts the bound peptide, compromises peptide-binding activity. We conclude that peptide binds to the concave face of the β sheet of the N-terminal domain, where binding is regulated during the action cycle of the chaperone.
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Details
- Title
- Identification of the N-terminal Peptide Binding Site of Glucose-regulated Protein 94
- Creators
- Tali Gidalevitz - University of ChicagoChhanda Biswas - University of ChicagoHua Ding - Children's Hospital of PhiladelphiaDina Schneidman-Duhovny - Tel Aviv UniversityHaim J. Wolfson - Tel Aviv UniversityFred Stevens - Argonne National LaboratorySheena Radford - University of LeedsYair Argon - University of Chicago
- Publication Details
- The Journal of biological chemistry, v 279(16), pp 16543-16552
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology; College of Arts and Sciences; Drexel University
- Web of Science ID
- WOS:000220747900104
- Scopus ID
- 2-s2.0-1942469336
- Other Identifier
- 991020099050504721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology