Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Article Abstract:

The structural adenosine triphosphate (ATP)/adenosine diphosphate-binding site in the Hsp90 heat shock protein was analyzed tp characterize the mechanisms of ATP binding and hydrolysis. Analysis of the yeast 90 kilodalton heat shock protein indicated the presence of an inherent adenosine triphosphatase activity in Hsp90. Furthermore, the yeast heat shock protein exhibited conformational changes in the presence of ATP.

Heat shock proteins, Protein binding, Binding sites (Biochemistry), Active sites (Biochemistry), Adenosine triphosphate, ATP

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The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50

Article Abstract:

The protein kinases are the largest coherent class of proteins amongst Hsp90s. Hsp90-dependent protein kinases in mammalian cells is associated with a 50kDa protein. Activation and maintenance of Hsp90 -dependent client proteins proceeds through an ordered sequence of complexes.

Science & research, Genetic aspects, Nucleotide sequence, Base sequence, Proteins, Protein kinases, Mammals, Genetic research

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