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The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains
Author(s) -
Mok Danny,
Allan Rudi K.,
Carrello Amerigo,
Wangoo Kiran,
Walkinshaw Malcolm D.,
Ratajczak Thomas
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.04.039
Subject(s) - tetratricopeptide , isomerase , cyclophilin , pin1 , peptidylprolyl isomerase , prolyl isomerase , chaperone (clinical) , chemistry , biochemistry , co chaperone , biology , computational biology , medicine , enzyme , heat shock protein , hsp90 , pathology , gene
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.