Structural and mechanistic consequences of polypeptide binding by GroEL

The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of proteins constitutes one of the most fascinating molecular recognition events in protein chemistry. Recent structural studies have revealed a possible model for substrate binding by GroEL and a high-r...

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Bibliographic Details
Published in:Folding & design 1997-01, Vol.2 (6), p.R93-R104
Main Authors: Coyle, Joseph E, Jaeger, Joachim, Groß, Michael, Robinson, Carol V, Radford, Sheena E
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Chaperonin 60 - chemistry
Chaperonin 60 - metabolism
Models, Molecular
Molecular Sequence Data
Peptides - chemistry
Peptides - metabolism
Protein Binding
Protein Conformation
Protein Folding
Structure-Activity Relationship
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Summary:The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of proteins constitutes one of the most fascinating molecular recognition events in protein chemistry. Recent structural studies have revealed a possible model for substrate binding by GroEL and a high-resolution image of the GroEL–GroES folding machinery has provided important new insights into our understanding of the mechanism of action of this chaperonin. Studies with a variety of model substrates reveal that the binding of substrate proteins to GroEL is not just a passive event, but can result in significant changes in the structure and stability of the bound polypeptide. The potential impact of this on the mechanism of chaperonin-assisted folding is not fully understood, but provides exciting scope for further experiment.
ISSN:1359-0278
1878-5808
DOI:10.1016/S1359-0278(97)00046-1