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Molecular chaperones: structure of a protein disaggregase.
- Source :
-
Current biology : CB [Curr Biol] 2004 Jan 20; Vol. 14 (2), pp. R78-80. - Publication Year :
- 2004
-
Abstract
- The ring-forming molecular chaperone Hsp104/ClpB is a member of the AAA+ protein family which rescues proteins from aggregated states. The newly determined crystal structure of ClpB provides new insights into the mechanism of protein disaggregation, suggesting a crowbar activity mediated by a unique coiled-coil domain.
- Subjects :
- Endopeptidase Clp
Escherichia coli metabolism
Escherichia coli Proteins metabolism
HSP70 Heat-Shock Proteins metabolism
Heat-Shock Proteins metabolism
Molecular Chaperones metabolism
Protein Structure, Tertiary physiology
Saccharomyces cerevisiae Proteins metabolism
Thermus thermophilus metabolism
Escherichia coli Proteins ultrastructure
Heat-Shock Proteins ultrastructure
Molecular Chaperones physiology
Protein Structure, Quaternary physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0960-9822
- Volume :
- 14
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Current biology : CB
- Publication Type :
- Academic Journal
- Accession number :
- 14738756
- Full Text :
- https://doi.org/10.1016/j.cub.2003.12.051