Peptidyl-prolyl cis-trans isomerase

Function

Peptidyl-prolyl cis-trans isomerase (PPIase) interconverts cis and trans isomers of proline. PPIase functions as a protein folding chaperone. The 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. The PPIase macrophage infectivity potentiator (Mip) is required for optimal infection of macrophages by some parasites. The PPIase SlyD acts as a chaperone and speeds up protein folding.

For various types of PPIase see:

• Cyclophilin
• FK506 binding protein
• The Escherichia coli sensitive to lysis D (SlyD) protein
• Multifaceted SlyD from Helicobacter pylori: implication in NiFe hydrogenase maturation

Disease

Relevance

Structural highlights