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Molecular chaperones: Clamps for the Clps?

descriptionPublicationkeyboard_double_arrow_right Article 01 Jun 1998 English Publisher:Elsevier BVJournal:Current Biology, volume 8, pages R464-R467 (issn: 0960-9822,

Authors: Lila M. Gierasch; Hwa-ping Feng;

doi: 10.1016/s0960-9822(98)70294-5

pmid: 9651675

Molecular chaperones: Clamps for the Clps?

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Abstract

The Clp/Hsp100 molecular chaperones are unusual in their ability to tease apart protein aggregates and complexes. Recent results make a good case that these chaperones bind substrates via PDZ-like domains; this may reflect a general strategy for manipulating the] assembly state of substrate proteins.

Related Organizations

University of Massachusetts System
United States
University of Massachusetts Amherst
United States

Keywords

Adenosine Triphosphatases, Models, Molecular, Protein Folding, Agricultural and Biological Sciences(all), Biochemistry, Genetics and Molecular Biology(all), Protein Conformation, Escherichia coli Proteins, Serine Endopeptidases, Protozoan Proteins, Endopeptidase Clp, Peptide Fragments, Protein Structure, Tertiary, Substrate Specificity, ATPases Associated with Diverse Cellular Activities, Heat-Shock Proteins, Molecular Chaperones

1 Research products, page 1 of 1

PDZ-like Domains Mediate Binding Specificity in the Clp/Hsp100 Family of Chaperones and Protease Regulatory Subunits
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