2024 Pin1 ww domain

Pin1 ww domain

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August undefined, 2024

WebFeb 16, 2001 · The WW domain-containing iso-prolyl isomerase named Pin1, a protein known to be essential for cell cycle progression, was shown to be active in restoration of … WebNational Center for Biotechnology Information

Molecules Free Full-Text Dynamic Allostery Modulates Catalytic ...

WebWW domains are small, 38 to 40 amino acid residue modules implicated in binding to Pro-rich sequences. WW domains and SH3 domains can potentially bind overlapping sites. In … WebSep 1, 2000 · The crystal structure of Pin1 bound to a phosphorylated peptide, via its WW domain, was solved by Verdecia et al. (PDB code 1F9A) (24). The peptide in that structure, which is derived from... rathkeova cista

Function of WW Domains as Phosphoserine- or Phosphothreonine ... - Science

WebMar 8, 2024 · We demonstrate that the phospho-Thr 335 -Pro motif serves as a putative binding site for the peptidyl-prolyl cis-trans isomerase (PPIase), Pin1, an enzyme that specifically recognizes peptide bonds at phospho-Ser/Thr-Pro motifs. WebAug 15, 2014 · SUMOylation of Pin1 on K6 in the WW domain and on K63 in the PPIase domain inhibits Pin1's activity and oncogenic function. SUMOylated Pin1 can be deSUMOylated by SUMO protease 1 (SENP1), which ... WebFeb 26, 1999 · WW domains are small protein modules found in various proteins that participate in cell signaling or regulation. WW domains of the essential mitotic prolyl … rath kadol

Frontiers Function of PIN1 in Cancer Development and Its …

WebPin1 is a two-domain cell regulator that isomerizes peptidyl-prolines. The catalytic domain (PPIase) and the other ligand-binding domain (WW) sample extended and compact conformations.... • Lu KP, Liou YC, Zhou XZ (Apr 2002). "Pinning down proline-directed phosphorylation signaling". Trends in Cell Biology. 12 (4): 164–72. doi:10.1016/S0962-8924(02)02253-5. PMID 11978535. • Wulf G, Finn G, Suizu F, Lu KP (May 2005). "Phosphorylation-specific prolyl isomerization: is there an underlying theme?". Nature Cell Biology. 7 (5): 435–41. doi:10.1038/ncb0505-435. PMID 15867923. S2CID 180385. dr razavi woodbridgeWebA hyperstable Pin1 WW domain has been circularly permuted via excision of the fold-nucleating turn; it still folds to form the native three-strand sheet and hydrophobic core features. Multiprobe folding dynamics studies of the normal and circularly permuted sequences, as well as their constituent hairpin fragments and comparable-length β ... rathke\u0027s pocket

"Web), Because the Pin1 WW domain mediates the substrate interaction of Pin1, it may determine the localization of Pin1 in the cell given that Pin1 is a 16-kDa protein small enough to … " - Pin1 ww domain

Pin1 ww domain

Stereospecific gating of functional motions in Pin1 PNAS

WebApr 12, 2005 · The rate-limiting step for human Pin1 WW domain folding is the formation of the loop 1 substructure. The native conformation of this six-residue loop positions side chains that are important for mediating protein-protein interactions through the binding of Pro-rich sequences. Replacement of the wild-type loop 1 primary structure by shorter ... WebPin1 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.

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WebThe WW domain, (also known as the rsp5-domain or WWP repeating motif) is a modular protein domain that mediates specific interactions with protein ligands. This domain is … WebFeb 19, 2001 · The WW domain-containing iso-prolyl isomerase named Pin1, a protein known to be essential for cell cycle progression, was shown to be active in restoration of the microtubule-binding activity of Tau, a protein of neurofibrillar tangles found in the brains of Alzheimer's patients. It is the WW domain of Pin1 that interacts directly with Tau protein.

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 interdomain communication; an isolated PPIase domain construct retains isomerase activity comparable to or greater than that of full-length Pin1, but full-length Pin1 shows different … WebThe complete phosphate binding module of the Pin1 WW domain encompasses the side chains of Ser 16, Arg 17, and Tyr 23 and the backbone amide of Arg 17. A bound water molecule mediates the...

WebJan 25, 2002 · Moreover, both Pin1 and WW domain mutants refractory to Ser(16) phosphorylation act as dominant-negative mutants to induce mitotic block and … WebThe best characterized pSer/Thr-binding WW domain is one in the peptidyl-prolyl isomerase (PPIase) Pin1 ( 4 , 7 ). Pin1 specifically isomerizes the pSer/Thr–Pro bond ( 8 , 9 , 10 ). Pin1 is essential for mitotic progression ( 11 , 12 , 13 ) and is required for the DNA replication checkpoint ( 14 ).

WebDownload scientific diagram The 3D structure of Pin1 with its postulated allosteric interaction within the variant WW domain. from publication: Protein Allostery at Atomic Resolution Protein ...

WebMay 28, 2015 · The WW domain from human Pin1, a proline isomerase involved in controlling cell proliferation, has been chosen as an exemplar since a number of fast … dr razavi wind gapWebAug 30, 2024 · Pin1 is part of the parvulin family of peptidyl-prolyl isomerases (PPIases), and it contains two distinct domains: the N-terminal WW domain and the catalytic C-terminal … rathke\\u0027s pocketWebOct 12, 2015 · Since target recognition of Pin1 is achieved by the interaction of the WW domain with the protein partners, we prepared an 15 N-labeled WW domain sample and monitored the chemical shift... rathleton plaza 2WebJul 11, 2011 · Pin1 is a modular protein of 163 residues consisting of a WW domain (1–39) and a larger peptidyl-prolyl isomerase (PPIase) domain (50–163) . A flexible linker … dr razavi wuppertalWebSep 3, 2012 · The human Pin1 WW domain is a small autonomously folding protein that has been useful as a model system for biophysical studies of β-sheet folding. This domain … dr raza white oakWebDownload scientific diagram The 3D structure of Pin1 with its postulated allosteric interaction within the variant WW domain. from publication: Protein Allostery at Atomic … rath kg bad kreuznachWebFeb 20, 2002 · The binding specificity between Pin1 WW domain and its target peptide is achieved by interactions between the phosphate group of one phosphorylated serine in the peptide and arginine and serine side-chains of the domain located in the first strand and in the β1–β2 loop. rathma\u0027s set