Article
Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain.
Nature structural & molecular biology - 1 Nov 2009
Tsutsumi Shinji, Mollapour Mehdi, Graf Christian, Lee Chung-Tien, Scroggins Bradley T, Xu Wanping, Haslerova Lenka, Hessling Martin, Konstantinova Anna A, Trepel Jane B, Panaretou Barry, Buchner Johannes, Mayer Matthias P, Prodromou Chrisostomos, Neckers Len
Abstract excerpt
Heat shock protein 90 (Hsp90) is an essential molecular chaperone in eukaryotes, as it regulates diverse signal transduction nodes that integrate numerous environmental cues to maintain cellular homeostasis. Hsp90 also is secreted from normal and transformed cells and regulates cell motility. Here, we have identified a conserved hydrophobic motif in a beta-strand at the boundary between the N domain and charged...
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