Title : In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.

Pub. Date : 1998 Nov 16

PMID : 9817749






1 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Based on a new crystal structure of the NH2-terminal domain of human Hsp90 with bound ADP-Mg and on the structural homology of this domain with the ATPase domain of Escherichia coli DNA gyrase, the residues of Hsp90 critical in ATP binding (D93) and ATP hydrolysis (E47) were identified. Adenosine Diphosphate heat shock protein 90 alpha family class A member 1 Homo sapiens