Pin1 ppiase
WebKPT-6566 is a selective and covalent prolyl isomerase PIN1 inhibitor, covalently binds to the catalytic site of PIN1, selectively inhibits and degrades PIN1. KPT-6566 shows an IC50 value of 640 nM and a K value of 625.2 nM for PIN1 PPIase domain. KPT-6566 can be used for the research of cancer . For research use only. We do not sell to patients.
Pin1 ppiase
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WebJan 1, 2024 · In solution, apo Pin1 adopts both extended and compact conformations (Born et al., 2024; Matena et al., 2013), the latter involving formation of the WW-PPIase interface. Only the compact Pin1 conformation, where the inter-domain interface is stabilized by a polyethylene glycol molecule (Ranganathan et al., 1997), is observed in all Pin1 crystal ... WebPin1 is a unique PPIase that specifically recognizes phosphorylated serine or threonine immediately preceding a proline residue (pSer/Thr-Pro), isomerizes the peptide bond, …
WebPin1 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]). WebPin1 consists of two domains: a N-terminal phosphor-peptide binding domain (WW domain) and a C-terminal catalytic domain (PPIase domain) (Figure 1A) [].Pin1 functions rely on …
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 ... Web2 beds, 1 bath, 1104 sq. ft. house located at 7801 Pine St, Pittsburgh, PA 15237. View sales history, tax history, home value estimates, and overhead views. APN ...
WebPin1 dysfunction is linked to an increasing number of human diseases, such as cancer and neurological disorders, including Alzheimer’s disease [ 5, 6, 7, 8, 9, 10 ]. Pin1 consists of two domains: a N-terminal phosphor-peptide binding domain (WW domain) and a C-terminal catalytic domain (PPIase domain) ( Figure 1 A) [ 11 ].
WebNational Center for Biotechnology Information office 365 kpeduWebAug 29, 2024 · Pin1 is the only known peptidyl-prolyl cis–trans isomerase (PPIase) that specifically recognizes and isomerizes the phosphorylated Serine/Threonine-Proline … office 365 koupitWebFeb 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 has many biological substrates, plays critical role in cell-cycle regulation, and up-regulated in many human cancers. Recently, Pin1 was linked to the Alzheimer’s disease pathogenesis. my charter login cincinnati children\u0027sWebOct 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 … my charter login chi omahaWebOct 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 … my charter login covenantWebPIN1 is a well-known PPIase that regulates the cis–trans isomerization of pSer/Thr–Pro, which highlights its importance in the control of Pro-directed phosphorylation. PIN1 … office 365 kostenlos online nutzenWebThe active site of the PPIase domain is highly conserved throughout the entire parvulin family, the subfamily of proline isomerases to which Pin1 belongs . The active site was identified in the structure of human Pin1 complexed with a low affinity dipeptide and is composed of a phosphate binding pocket, a prolyl binding pocket, and reaction ... my charter login cleve