Abstract
Chaperonins in the eukaryotic cytosol are more mysterious than their bacterial counterparts, with a heterogeneity of protein binding surfaces. In a recent issue of Molecular Cell, showed that binding specificity in the TRiC chaperonin is less than absolute and resolved the location of substrate binding surfaces in this chaperonin.
MeSH terms
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Adenosine Triphosphatases / chemistry
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Archaeal Proteins / metabolism
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Binding Sites
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Chaperonin 60 / chemistry
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Chaperonin Containing TCP-1
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Chaperonins / metabolism
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Chaperonins / physiology*
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Cytoplasm / metabolism
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Cytosol / metabolism
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Escherichia coli / metabolism
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Models, Biological
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Molecular Chaperones
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Protein Binding
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Protein Conformation
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Protein Folding
Substances
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Archaeal Proteins
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Chaperonin 60
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Molecular Chaperones
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Adenosine Triphosphatases
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Chaperonin Containing TCP-1
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Chaperonins