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Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases.
FEBS Lett. 2001 Apr 20; 495(1-2):1-6.FL

Abstract

Receptor accessory peptidyl prolyl cis/trans isomerases (PPIases) of the FKBP and cyclophilin types form receptor heterocomplexes with different stabilities. PPIases have been found to associate with other receptor heterocomplex constituents via either proline-directed active sites or additional domains of the enzymes. The single-domain PPIases FKBP12 and FKBP12.6 are shown to interact with receptor protein kinases and calcium channels at their active sites. In contrast, heterooligomeric nuclear receptors contain multi-domain PPIases like FKBP51, FKBP52 or cyclophilin 40 that directly interact with the chaperone hsp90 via the tetratricopeptide repeat modules of the folding helper enzymes. PPIases play a critical role in the functional arrangement of components within receptor heterocomplexes.

Authors+Show Affiliations

Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120, Halle/Saale, Germany. schiene@enzyme-halle.mpg.deNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

11322937

Citation

Schiene-Fischer, C, and C Yu. "Receptor Accessory Folding Helper Enzymes: the Functional Role of Peptidyl Prolyl Cis/trans Isomerases." FEBS Letters, vol. 495, no. 1-2, 2001, pp. 1-6.
Schiene-Fischer C, Yu C. Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. FEBS Lett. 2001;495(1-2):1-6.
Schiene-Fischer, C., & Yu, C. (2001). Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. FEBS Letters, 495(1-2), 1-6.
Schiene-Fischer C, Yu C. Receptor Accessory Folding Helper Enzymes: the Functional Role of Peptidyl Prolyl Cis/trans Isomerases. FEBS Lett. 2001 Apr 20;495(1-2):1-6. PubMed PMID: 11322937.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. AU - Schiene-Fischer,C, AU - Yu,C, PY - 2001/4/27/pubmed PY - 2001/5/25/medline PY - 2001/4/27/entrez SP - 1 EP - 6 JF - FEBS letters JO - FEBS Lett VL - 495 IS - 1-2 N2 - Receptor accessory peptidyl prolyl cis/trans isomerases (PPIases) of the FKBP and cyclophilin types form receptor heterocomplexes with different stabilities. PPIases have been found to associate with other receptor heterocomplex constituents via either proline-directed active sites or additional domains of the enzymes. The single-domain PPIases FKBP12 and FKBP12.6 are shown to interact with receptor protein kinases and calcium channels at their active sites. In contrast, heterooligomeric nuclear receptors contain multi-domain PPIases like FKBP51, FKBP52 or cyclophilin 40 that directly interact with the chaperone hsp90 via the tetratricopeptide repeat modules of the folding helper enzymes. PPIases play a critical role in the functional arrangement of components within receptor heterocomplexes. SN - 0014-5793 UR - https://www.unboundmedicine.com/medline/citation/11322937/Receptor_accessory_folding_helper_enzymes:_the_functional_role_of_peptidyl_prolyl_cis/trans_isomerases_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-5793(01)02326-2 DB - PRIME DP - Unbound Medicine ER -