Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants.

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Article

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants.

The Journal of biological chemistry - 29 Apr 1994

Wilbanks S M, DeLuca-Flaherty C, McKay D B

Abstract excerpt

The 70-kDa heat shock cognate protein is a member of a highly conserved family of molecular chaperones in which the binding and release of target polypeptides are coupled to the chaperones' ATPase activity. The ATPase activity resides in the amino-terminal 44-kDa fragment of the protein. Four aci...

Topics

Adenosine Triphosphate
Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Carrier Proteins
Cattle
DNA, Complementary
HSC70 Heat-Shock Proteins
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Hydrolysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Magnesium

Molecular Sequence Data

Mutation

Protein Conformation

Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 8175706

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8175706-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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