Article
Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex.
Nature structural & molecular biology - 1 Feb 2005
Xu Wanping, Yuan Xitong, Xiang Zhexin, Mimnaugh Edward, Marcu Monica, Neckers Len
Abstract excerpt
The molecular chaperone Hsp90 modulates the function of specific cell signaling proteins. Although targeting Hsp90 with the antibiotic inhibitor geldanamycin (GA) may be a promising approach for cancer treatment, little is known about the determinants of Hsp90 interaction with its client proteins. Here we identify a loop within the N lobe of the kinase domain of ErbB2 that determines Hsp90 binding. The amino acid...
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