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....

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Bibliographic Details
Published inCurrent biology Vol. 9; no. 8; pp. R305 - R308
Main Author Kelley, William L.
Format Journal Article
LanguageEnglish
Published England Elsevier Inc 22.04.1999
Subjects
Binding Sites
Escherichia coli
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - metabolism
Heat-Shock Proteins - physiology
HSP40 Heat-Shock Proteins
HSP70 Heat-Shock Proteins - metabolism
Molecular Chaperones - metabolism
Molecular Chaperones - physiology
Protein Binding
Protein Structure, Tertiary
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Summary: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.
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ISSN:0960-9822
1879-0445
DOI:10.1016/S0960-9822(99)80185-7