PIN1 Human

PIN1 was first identified in 1996 by Lu et al. It belongs to the parvulins subfamily of peptidyl-prolyl cis/trans isomerases (PPIases) . The enzyme consists of two distinct domains: an N-terminal WW domain that binds to phosphorylated Ser/Thr-Pro motifs and a C-terminal PPIase domain that catalyzes the isomerization reaction .

The isomerization of peptidyl-prolyl bonds by PIN1 induces conformational changes in target proteins, acting as a molecular switch in multiple cellular processes . This conformational regulation has a profound impact on key proteins involved in cell growth, stress responses, immune response, pluripotency, germ cell development, neuronal differentiation, and survival .

PIN1 is overexpressed in various human cancers, driving oncogenesis by modulating oncogene and tumor suppressor activity . It has also been implicated in the pathogenesis of Alzheimer’s disease and other neurodegenerative disorders . The enzyme’s ability to regulate protein conformation after phosphorylation makes it a critical player in these diseases.

Given its significant role in cancer and neurodegenerative diseases, PIN1 has been a target for therapeutic intervention. Recent studies have identified potent and specific covalent inhibitors of PIN1, such as Sulfopin, which have shown promising results in reducing tumor progression and increasing survival in mouse models of cancer .

Human recombinant PIN1 is produced using recombinant DNA technology, which involves inserting the PIN1 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study the enzyme’s function, mechanism, and potential therapeutic targets.