parvulin

Parvulins are a family of immunophilins, which are a group of proteins that bind to immunosuppressants. Like other immunophilins, parvulins are thought to act as peptidyl-prolyl cis-trans isomerases, enzymes that catalyze the isomerization of proline-containing peptide bonds. This isomerization is a critical step in protein folding and is important for the proper function of many proteins.

The parvulin family includes several distinct members, such as Pin1, Ess1, and Par14. Pin1, in particular, has been extensively studied and is known to regulate the activity of numerous proteins involved in cell cycle progression, DNA repair, and signaling pathways. Its ability to specifically recognize phosphorylated serine or threonine residues followed by a proline residue makes it a crucial regulator of protein function.

Parvulins are found in a wide range of organisms, from bacteria to humans, indicating their fundamental biological role. Their involvement in diverse cellular processes suggests their importance in maintaining cellular homeostasis and responding to various stimuli. Dysregulation of parvulin activity has been implicated in several diseases, including cancer and neurodegenerative disorders, making them potential therapeutic targets. Research into parvulins continues to uncover their complex roles in cellular biology and disease pathogenesis.