2m0z | pdb_00002m0z

cis form of a photoswitchable PDZ domain crosslinked with an azobenzene derivative

spinqualitylabelsall models 2m0z, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2m0z is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 33B Related: 2m10 Gene: PTPN13, PNP1, PTP1E, PTPL1 (Homo sapiens) Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PTN13_HUMAN] Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling. Publication Abstract from PubMed By covalently linking an azobenzene photoswitch across the binding groove of a PDZ domain, a conformational transition, similar to the one occurring upon ligand binding to the unmodified domain, can be initiated on a picosecond timescale by a laser pulse. The protein structures have been characterized in the two photoswitch states through NMR spectroscopy and the transition between them through ultrafast IR spectroscopy and molecular dynamics simulations. The binding groove opens on a 100-ns timescale in a highly nonexponential manner, and the molecular dynamics simulations suggest that the process is governed by the rearrangement of the water network on the protein surface. We propose this rearrangement of the water network to be another possible mechanism of allostery. Kinetic response of a photoperturbed allosteric protein.,Buchli B, Waldauer SA, Walser R, Donten ML, Pfister R, Blochliger N, Steiner S, Caflisch A, Zerbe O, Hamm P Proc Natl Acad Sci U S A. 2013 Jul 1. PMID:23818626 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase

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