PMID:9428517

Citation	Levchenko, I, Smith, CK, Walsh, NP, Sauer, RT and Baker, TA (1997) PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell 91:939-47
Abstract	ClpX, a molecular chaperone and the regulatory subunit of the ClpXP protease, is shown to contain tandem modular domains that bind to the C-terminal sequences of target proteins in a manner that parallels functional specificity. Nuclear magnetic resonance studies show that these C-terminal sequences are displayed as disordered peptides on the surface of otherwise folded proteins. The ClpX substrate-binding domains are homologous to sequences in other Clp/Hsp100 proteins and are related more distantly to PDZ domains, which also mediate C-terminal specific protein-protein interactions. Conservation of these binding domains indicates that the mode of substrate recognition characterized here for ClpX will be a conserved feature among Clp/Hsp100 family members and a distinguishing characteristic between this chaperone family and the Hsp70 chaperones.
Links	PubMed
Keywords	Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Binding Sites; Endopeptidase Clp; Escherichia coli; Escherichia coli Proteins; Heat-Shock Proteins/metabolism; Magnetic Resonance Spectroscopy; Molecular Chaperones/metabolism; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Folding; Protozoan Proteins/metabolism; Serine Endopeptidases/metabolism
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