PMID:14962378

Citation	Maurizi, MR and Xia, D (2004) Protein binding and disruption by Clp/Hsp100 chaperones. Structure 12:175-83
Abstract	Clp/Hsp100 chaperones work with other cellular chaperones and proteases to control the quality and amounts of many intracellular proteins. They employ an ATP-dependent protein unfoldase activity to solubilize protein aggregates or to target specific classes of proteins for degradation. The structural complexity of Clp/Hsp100 proteins combined with the complexity of the interactions with their macromolecular substrates presents a considerable challenge to understanding the mechanisms by which they recognize and unfold substrates and deliver them to downstream enzymes. Fortunately, high-resolution structural data is now available for several of the chaperones and their functional partners, which together with mutational data on the chaperones and their substrates has provided a glimmer of light at the end of the Clp/Hsp100 tunnel.
Links	PubMed Online version:10.1016/j.str.2004.01.021
Keywords	Heat-Shock Proteins/chemistry; Molecular Chaperones/chemistry; Protein Binding; Protein Folding; Protein Structure, Tertiary/physiology; Protein Subunits/chemistry; Protozoan Proteins/chemistry
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