Pin1 ppiase
WebOct 15, 2001 · Pin1/Ess1p is a highly conserved WW domain-containing peptidyl-prolyl isomerase (PPIase); its WW domain binds specifically to phospho-Ser/Thr-Pro sequences and its catalytic domain isomerizes phospho-Ser/Thr-Pro bonds. Pin1 PPIase activity can alter protein conformation in a phosphorylation-dependent manner and/or promote … WebAug 29, 2024 · Pin1 is the only known peptidyl-prolyl cis–trans isomerase (PPIase) that specifically recognizes and isomerizes the phosphorylated Serine/Threonine-Proline …
Pin1 ppiase
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WebOct 1, 2009 · Originally identified in a yeast two-hybrid screen, Pin1 (Protein Interacting with NIMA) interacts physically and functionally with the mitotic kinase NIMA (Never In Mitosis gene A). 1 Pin1 is a member of peptidyl-prolyl cis–trans isomerase (PPIase) family. 1 Pin1 substrate proteins are important in cell-cycle regulation and are commonly deregulated in … WebJun 9, 2024 · (b) Bar plot indicating PPIase activity K of PIN1 (black), PIN1 S67E (white) and PIN1 with 30 μM of the indicated compounds. Positive hit is marked in bold. Positive hit is marked in bold.
WebFeb 13, 2024 · Pin1 consists of short N-terminal protein-protein interaction domain that allows enzyme to bind phosphoproteins and longer C-terminal izomerase domain. Pin1 … WebDec 12, 1997 · Pin1, originally isolated as a protein that interacts with and inhibits the essential mitotic kinase NIMA, is highly conserved and possesses both a WW domain …
WebMay 30, 2024 · The PPIase activity on GST-Pin1 in response to ATRA and 1,25-(OH) 2 vitamin D3 were determined using the chymotrypsin-coupled PPIase activity assay with … WebApr 30, 2024 · Pin1, a key PPIase in the cell, recognizes a phosphorylated Ser/Thr-Pro motif to catalyze peptidyl-prolyl isomerization in proteins. The significance of the phosphorylation-dependent Pin1 activity was recently highlighted for isomerization of ATR ( ataxia telangiectasia - and Rad3-related).
WebPIN1-catalyzed conformational regulation has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune …
WebSep 23, 2024 · KPT-6566 covalently binds to PIN1 PPIase, and inhibits the PPIase activity of PIN1, with an IC50 of 0.64 μM. It selectively inhibits PIN1 instead of other PPIases. KPT-6566 does not affect the PPIase activity of recombinant GST-FKBP4 and GST-PPIA, which also own cysteine residues. In a further study, it proves that KPT-6566 affects PIN1 ... blue orchid charlotte ncWebPin1 is a unique PPIase that specifically recognizes phosphorylated serine or threonine immediately preceding a proline residue (pSer/Thr-Pro), isomerizes the peptide bond, and is known to play an important role in cell cycle progression (reviewed in [68,70]). clearinghouse diplomaWebJul 11, 2011 · Pin1 is a reversible enzyme that catalyzes the cis - trans isomerization of the pS/T-P imide linkages ( 2, 3) of other signaling proteins, such as CDC25C, p53, c-Myc, NF-kB, cyclin D1, and tau ( 3 ). Pin1 engages when external events, such as S/T (de)-phosphorylation, change the cis - trans equilibrium. clearinghouse dodWebPin1 Protein Overview Peptidyl-prolyl cis/trans isomerases (PPIases; EC 5.2.1.8), such as PIN1, catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. PIN1 is the only PPIase that specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. blue orchid chinese numberWebPin 1, or peptidyl-prolyl cis/trans isomerase (PPIase), isomerizes only phospho-Serine/Threonine-Proline motifs. The enzyme binds to a subset of proteins and thus … blue orchid cookie runWebOct 23, 2024 · The purified full-length Pin1 protein contains 163 amino acids, plus the residues in the His tag. The backbone and side-chain chemical shifts of apo Pin1 were assigned manually, with aid from previously published shift lists of the isolated WW (residues 1–39) and PPIase domains (residues 50–163), and the backbone assignment of full … blue orchid borderWebAug 9, 2024 · The PPIase activity on GST-Pin1, GST-FKBP12, or GST-cyclophilin in response to ATO were determined using the chymotrypsin-coupled PPIase activity assay with the substrate Suc-Ala-pSer-Pro-Phe-pNA ... clearinghouse driver login