EC Number   |
|---|
   3.4.19.12 | at 2.4 A resolution, x-ray crystallography. Overall fold resembles that of other ubiquitin hydrolases, including UCHL3. Geometry of the catalytic residues in the active site of UCH-L1 is distorted in such a way that the hydrolytic activity appears to be impossible without substrate induced conformational rearrangements |
| 3.4.19.12 | hanging drop vapour diffusion method, 1.45 A resolution crystal structure of human UCH-L3 in complex with the inhibitor ubiquitin vinylmethyl ester |
| 3.4.19.12 | hanging drop vapour diffusion method, 3.1 A resolution crystal structure of the PLP2 domain originating from PEDV polyprotein 1a bound to ubiquitin |
| 3.4.19.12 | purified recombinant UCH37 catalytic domain, i.e. UCH37N, selenomethionine-substituted UCH37N, and of mutant C88A, sitting-drop vapor diffusion method, 14 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 1 mM DTT, 20°C, versus a reservoir solution containing 22% PEG 4000, 0.2 M MgCl2, 0.1 M Tris-HCl, pH 8.5, and 3.5% xylitol, microseeding, X-ray diffraction structure determination and analysis at 2.2 A resolution |
| 3.4.19.12 | purified recombinant wild-type and mutant GST-tagged enzymes, 35 mg/ml protein in 50 mM Tris-HCl, pH 7.4, 150 mM NaCl, 10 mM DTT, crystallization at room temperature, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular modeling, structure-function relationship |
| 3.4.19.12 | purified recombinant wild-type UCH-L1 and the Parkinson disease-associated variant of the enzyme, mutant S18Y, bound to a ubiquitin-based suicide substrate, ubiquitin vinyl methyl ester, hanging drop vapour diffusion method, 25 mg/ml enzyme-UbVMe complex in 50 mM Tris-HCl, pH 7.4, 150 mM NaCl, and 10 mM DTT, are mixed with 2.4 M ammonium sulfate and 0.1 M bicine, pH 9.0, 2 months, X-ray diffraction structure determination and analysis at 2.4-2.85 A resolution, molecular replacement |
| 3.4.19.12 | UCH-L3, crystal structure at 1.8 A resolution |
| 3.4.19.12 | X-ray structure of UCHL1 co-crystallized with a peptide-based fluoromethylketone inhibitor, benzyloxycarbonyl-Val-Ala-Glu(gamma-methoxy) fluoromethylketone (Z-VAE(OMe)-FMK (VAEFMK)), at 2.35 A resolution is reported |
