2vwc

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

Structural highlights 2vwc is a 1 chain structure with sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 2vls. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Related: 1hk7, 1a4h, 1us7, 2bre, 2cg9, 1ah6, 1usv, 1bgq, 2iws, 1amw, 2brc, 1zwh, 1usu, 2vw5, 1ah8, 2cgf, 2iwu, 1am1, 2iwx, 2cge, 1zw9, 2akp Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Proteins

spinqualitylabelsall models 2vwc, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image