Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization.

Allan, Rudi K; Mok, Danny; Ward, Bryan K; Ratajczak, Thomas

Allan, Rudi K; Mok, Danny; Ward, Bryan K; Ratajczak, Thomas.

Affiliation

Allan RK; Laboratory for Molecular Endocrinology, Western Australian Institute for Medical Research, Queen Elizabeth II Medical Centre, The University of Western Australia, Hospital Avenue, Nedlands, WA 6009, Australia.

J Biol Chem ; 281(11): 7161-71, 2006 Mar 17.

Article in En | MEDLINE | ID: mdl-16421106

Subject(s)

Anti-Bacterial Agents/chemistry; Coumarins/chemistry; HSP90 Heat-Shock Proteins/chemistry; Molecular Chaperones/chemistry; Novobiocin/chemistry; Alanine/chemistry; Amino Acid Sequence; Aminocoumarins/chemistry; Binding Sites; DNA, Complementary/metabolism; Dimerization; Dose-Response Relationship, Drug; Enzyme Inhibitors/chemistry; Enzyme-Linked Immunosorbent Assay; Glutathione Transferase/metabolism; HeLa Cells; Humans; Immunophilins/chemistry; Molecular Conformation; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Plasmids/metabolism; Point Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Steroids/chemistry; Substrate Specificity; Tacrolimus Binding Proteins/chemistry; Time Factors

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PubMed Links

Database: MEDLINE Main subject: Novobiocin / Molecular Chaperones / HSP90 Heat-Shock Proteins / Coumarins / Anti-Bacterial Agents Limits: Humans Language: En Year: 2006 Type: Article

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