Molecular chaperones: How J domains turn on Hsp70s

Kelley, William

doi:10.1016/s0960-9822(99)80185-7

Scientific article

English

Molecular chaperones: How J domains turn on Hsp70s

ContributorsKelley, William

Published inCurrent biology, vol. 9, no. 8, p. R305-308

Publication date1999

Abstract

Molecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules.

Keywords

Binding Sites
HSP40 Heat-Shock Proteins
HSP70 Heat-Shock Proteins/metabolism
Heat-Shock Proteins/chemistry/metabolism/physiology
Molecular Chaperones/metabolism/ physiology
Protein Binding
Protein Structure, Tertiary

Affiliation entities

Faculté de médecine / Section de médecine clinique / Département de médecine

Citation (ISO format)

KELLEY, William. Molecular chaperones: How J domains turn on Hsp70s. In: Current biology, 1999, vol. 9, n° 8, p. R305–308. doi: 10.1016/s0960-9822(99)80185-7

Article

Identifiers

PID : unige:7377
DOI : 10.1016/s0960-9822(99)80185-7
PMID : 10226023

Journal ISSN0960-9822

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Molecular chaperones: How J domains turn on Hsp70s

Molecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules.

Technical informations