Peptidyl-prolyl cis-trans isomerase

spinqualitylabelsall models Human PPIase (green) complex with phosphoserine containing peptide (magenta) (PDB code 1f8a). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Peptidyl-prolyl cis-trans isomerase (PPIase) interconverts cis and trans isomers of proline. PPIase functions as a protein folding chaperone. PPIase Pin1 isomerizes phospho-serine/threonine proline motifs. The deregulation of Pin1 may be involved in cancer and Alzheimer Disease. Pin1 consists of 2 domains: the WW domain recognizes the pSer/pThr Pro motif and the PPIase domain contains the catalytic site. PPIase PinA is an archaeal parvulin-like PPIase. PPIase Mip (macrophage infectivity potentiator) is required for optimal infection of macrophages by some parasites. PPIase SlyD acts as a chaperone and speeds up protein folding. PPIase SlpA is a 2-domain protein containing an FK506-binding domain and a PPIase domain and a small insert-in-flap domain which acts as a chaperone. For various types of PPIase see: • Cyclophilin • FK506 binding protein for SlyD • The Escherichia coli sensitive to lysis D (SlyD) protein • Multifaceted SlyD from Helicobacter pylori: implication in NiFe hydrogenase maturation Disease Mutations in PPIase genes are associated with age-related diseases like cardiovascular diseases, atherosclerosis, diabetes type II, chronic kidney disease, neurodegredation, cancer and age-related macular degeneration. Structural highlights The phosphoserine containing peptide found in the heptad repeat of RNA polymerase II large subunit interacts with the WW domain of PPIase Pin1. The phosphoserine containing peptide binding site. Water molecules are shown as red spheres. 3D Structures of peptidyl-prolyl cis-trans isomerase Peptidyl-prolyl cis-trans isomerase 3D structures

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