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Free keywords:
CIS-TRANS ISOMERIZATION; COLI TRIGGER FACTOR; HEAT-SHOCK-PROTEIN;
MOLECULAR CHAPERONE FUNCTIONS; PROLYL ISOMERASE DOMAIN;
CYCLOSPORINE-A-BINDING; GLUCOCORTICOID-RECEPTOR; CYCLOPHILIN-A;
FK506-BINDING PROTEIN-51; CONFORMATIONAL DYNAMICSBiochemistry & Molecular Biology; Life Sciences & Biomedicine - Other
Topics; chaperones; FKBP5; FKBP51; FKBP52; Peptidylprolylisomerases;
Abstract:
Peptidylprolyl-isomerases (PPIases) comprise of the protein families of FK506 binding proteins (FKBPs), cyclophilins, and parvulins. Their common feature is their ability to expedite the transition of peptidylprolyl bonds between thecisand thetransconformation. Thus, it seemed highly plausible that PPIase enzymatic activity is crucial for protein folding. However, this has been difficult to prove over the decades since their discovery. In parallel, more and more studies have discovered scaffolding functions of PPIases. This essay discusses the hypothesis that PPIase enzymatic activity might be the consequence of binding to peptidylprolyl protein motifs. The main focus of this paper is the large immunophilins FKBP51 and FKBP52, but other PPIases such as cyclophilin A and Pin1 are also described. From the hypothesis, it follows that the PPIase activity of these proteins might be less relevant, if at all, than the organization of protein complexes through versatile protein binding. Also see the video abstract here .
