The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains
Copyright policy )The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains
Cyclophilin 40 (CyP40), an immunophilin cochaperone present in steroid receptor‐Hsp90 complexes, contains an N‐terminal peptidylprolyl isomerase (PPIase) domain separated from a C‐terminal Hsp90‐binding tetratricopeptide repeat (TPR) domain by a 30‐residue linker. To map CyP40 chaperone function, CyP40 deletion mutants were prepared and analysed for chaperone activity. CyP40 fragments containing the PPIase domain plus linker or the linker region and the adjoining TPR domain retained chaperone activity, whilst individually, the catalytic and TPR domains were devoid of chaperoning ability. CyP40 chaperone function then, is localized within the linker that forms a binding cleft with potential to accommodate non‐native substrates.
- University of Western Australia Australia
- Sir Charles Gairdner Hospital Australia
- Universities Australia Australia
- University of Edinburgh United Kingdom
- Sir Charles Gairdner Osborne Park Health Care Group Australia
Models, Molecular, Protein Denaturation, Cyclophilin 40, Molecular Sequence Data, Tetratricopeptide repeat domain, Protein Structure, Tertiary, Cyclophilins, Chaperone activity, Animals, Peptidyl-Prolyl Isomerase F, Humans, Peptidylprolyl isomerase, Cattle, Heat shock protein 90, Amino Acid Sequence, HSP90 Heat-Shock Proteins, Peptides, Hydrophobic and Hydrophilic Interactions, Sequence Alignment, Conserved Sequence, Molecular Chaperones, Protein Binding
Models, Molecular, Protein Denaturation, Cyclophilin 40, Molecular Sequence Data, Tetratricopeptide repeat domain, Protein Structure, Tertiary, Cyclophilins, Chaperone activity, Animals, Peptidyl-Prolyl Isomerase F, Humans, Peptidylprolyl isomerase, Cattle, Heat shock protein 90, Amino Acid Sequence, HSP90 Heat-Shock Proteins, Peptides, Hydrophobic and Hydrophilic Interactions, Sequence Alignment, Conserved Sequence, Molecular Chaperones, Protein Binding
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