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Acta Cryst. (2014). A70, C804
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Human heat shock protein 27 (Hsp27) is an oligomeric and cell survival protein that has been associated with several cancers including prostrate and breast cancer. It's a known anti-apoptotic protein that functions as a molecular chaperone for several proteins. Hsp27 characteristically binds and stabilizes numerous partially unfolded proteins preventing their degradation, and has been shown to prevent actin polymerization in vitro. Several actin-binding residues involved in this interaction have been identified at the N-terminal loop and highly conserved alpha crystallin domains of Hsp27. Multiple assays have demonstrated that this hydrophobic actin-binding site is also involved in other protein binding. We therefore propose a common substrate-binding region on Hsp27 and present a model of Hsp27 binding to actin.
Keywords: Hsp27; Actin; crystallin.

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