Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond pr ...
The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function [1].
Peptidyl-prolyl cis-trans isomerase CYP38 from Arabidopsis is required for the assembly and stabilization of PSII [1]. It consists of an N-terminal helical bundle and a C-terminal cyclophilin beta-barrel (Pfam:PF00160)[1]. This entry represents the N ...
Peptidyl-prolyl cis-trans isomerase CYP38 from Arabidopsis is required for the assembly and stabilization of PSII [1]. It consists of an N-terminal helical bundle and a C-terminal cyclophilin beta-barrel (Pfam:PF00160)[1]. This entry represents the N-terminal helical bundle found in Cyp37/38 from Arabidopsis and similar proteins from cyanobacteria. This domain establishes strong interactions with the C-terminal domain to avoid the access of the cyclophilin domain to other proteins [1].
