| 11375525 |
Rodrigues ML, Archer M, Bonifacio MJ, Soares-da-Silva P, Carrondo MA: Crystallization and preliminary crystallographic characterization of catechol-O-methyltransferase in complex with its cosubstrate and an inhibitor. Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):906-8. Epub 2001 May 25.
Catechol-O-methyltransferase (COMT) is involved in the metabolism of catecholamines, catechol steroids and xenobiotic catechols. A precise knowledge of the enzyme-inhibitor structural interactions could help in the design of better inhibitors. Soluble rat COMT was expressed in Escherichia coli and the recombinant protein was crystallized with a new tight-binding inhibitor, BIA 3-335 [1-(3,4-dihydroxy-5-nitrophenyl)-3-(n-3'-trifluoromethylphenyl) piperazine- 1-propanone dihydrochloride]. The crystals were obtained by the sitting-drop vapour-diffusion method using PEG 6K as a precipitant. These crystals diffracted to better than 1.9 A and belong to the trigonal space group P3 (2) 21. The unit-cell parameters for the crystal measured at room temperature were a = b = 51.5, c = 168.3 A; each shrank by about 1 A on freezing. |
33(0,1,1,3) |