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The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains.
FEBS Lett. 2006 May 15; 580(11):2761-8.FL

Abstract

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.

Authors+Show Affiliations

Laboratory for Molecular Endocrinology, Western Australian Institute for Medical Research and UWA Centre for Medical Research, The University of Western Australia, Nedlands, WA 6009, Australia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16650407

Citation

Mok, Danny, et al. "The Chaperone Function of Cyclophilin 40 Maps to a Cleft Between the Prolyl Isomerase and Tetratricopeptide Repeat Domains." FEBS Letters, vol. 580, no. 11, 2006, pp. 2761-8.
Mok D, Allan RK, Carrello A, et al. The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains. FEBS Lett. 2006;580(11):2761-8.
Mok, D., Allan, R. K., Carrello, A., Wangoo, K., Walkinshaw, M. D., & Ratajczak, T. (2006). The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains. FEBS Letters, 580(11), 2761-8.
Mok D, et al. The Chaperone Function of Cyclophilin 40 Maps to a Cleft Between the Prolyl Isomerase and Tetratricopeptide Repeat Domains. FEBS Lett. 2006 May 15;580(11):2761-8. PubMed PMID: 16650407.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains. AU - Mok,Danny, AU - Allan,Rudi K, AU - Carrello,Amerigo, AU - Wangoo,Kiran, AU - Walkinshaw,Malcolm D, AU - Ratajczak,Thomas, Y1 - 2006/04/24/ PY - 2006/03/28/received PY - 2006/04/08/accepted PY - 2006/5/3/pubmed PY - 2006/7/6/medline PY - 2006/5/3/entrez SP - 2761 EP - 8 JF - FEBS letters JO - FEBS Lett VL - 580 IS - 11 N2 - 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. SN - 0014-5793 UR - https://www.unboundmedicine.com/medline/citation/16650407/The_chaperone_function_of_cyclophilin_40_maps_to_a_cleft_between_the_prolyl_isomerase_and_tetratricopeptide_repeat_domains_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-5793(06)00474-1 DB - PRIME DP - Unbound Medicine ER -