Novobiocin and Related Coumarins and Depletion of Heat Shock Protein 90-Dependent Signaling Proteins | Zendy

Monica G. Marcu | Zendy; T W Schulte | Zendy; Leonard Μ. Neckers | Zendy

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Novobiocin and Related Coumarins and Depletion of Heat Shock Protein 90-Dependent Signaling Proteins

Author(s) -

Monica G. Marcu,

T W Schulte,

Leonard Μ. Neckers

Publication year - 2000

Publication title -

jnci journal of the national cancer institute

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.797

H-Index - 356

eISSN - 1460-2105

pISSN - 0027-8874

DOI - 10.1093/jnci/92.3.242

Subject(s) - novobiocin , geldanamycin , hsp90 , dna gyrase , heat shock protein , biochemistry , biology , chemistry , microbiology and biotechnology , escherichia coli , antibiotics , gene

Heat shock protein 90 (Hsp90) interacts with and stabilizes several oncogenic protein kinases (e.g., p185(erbB2), p60(v-src), and Raf-1) and is required for the stability and dominant-negative function of mutated p53 protein. Two unrelated antibiotics, geldanamycin and radicicol, bind specifically to an atypical nucleotide-binding pocket of Hsp90, a site that shares homology with the adenosine triphosphate (ATP)-binding domain of bacterial DNA gyrase B. This interaction leads to destabilization of proteins that interact with Hsp90. Since the nucleotide-binding site of gyrase B is targeted by coumarin antibiotics (e.g., novobiocin), we investigated whether these drugs can also interact with Hsp90 and affect its activity.

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