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2vls

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Image:2vls.jpg

Template:STRUCTURE 2vls

STRUCTURE OF THE HSP90 INHIBITOR MACBECIN BOUND TO THE N-TERMINUS OF YEAST HSP90.


Overview

Macbecin compares favorably to geldanamycin as an Hsp90 inhibitor, being more soluble, stable, more potently inhibiting ATPase activity (IC 50 = 2 microM) and binding with higher affinity ( K d = 0.24 microM). Structural studies reveal significant differences in their Hsp90 binding characteristics, and macbecin-induced tumor cell growth inhibition is accompanied by characteristic degradation of Hsp90 client proteins. Macbecin significantly reduced tumor growth rates (minimum T/ C: 32%) in a DU145 murine xenograft. Macbecin thus represents an attractive lead for further optimization.

About this Structure

2VLS is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Molecular Characterization of Macbecin as an Hsp90 Inhibitor., Martin CJ, Gaisser S, Challis IR, Carletti I, Wilkinson B, Gregory M, Prodromou C, Roe SM, Pearl LH, Boyd SM, Zhang MQ, J Med Chem. 2008 Mar 22;. PMID:18357975

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