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Results 1 - 8 of 8
EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4complex of the D30N mutant enzyme with the statine-based inhibitor LP-149 as well as with a substrate based on a modification of the inhibitor, LP-149S 647828
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4crystal structure (1.7 A) of FIV protease is obtained in which 12 critical residues around the active site have been substituted with the structurally equivalent residues of HIV PR (12XFIV PR). The chimeric PR is crystallized in complex with inhibitor TL-3. Comparison of the crystal structures of the TL-3 complexes of 12X FIV and wild-type FIV PR reveal the information of additional van der Waals interactions between the enzyme inhibitor in the mutant PR 682828
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4crystal structure determination and analysis, recombinant enzyme 668799
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4hanging-drop vapor diffusion technique, crystals are grown at 4°C, crystal structure of the enzyme in complex with LP-130 647822
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4mutant I37V/N55M/V59I/I98S/Q99V/P100N in complex with HIV inhibitors darunavir and lopinavir, to 1.7 and 1.8 A resolution, respectively. A flexible 90s loop and residue 98 play roles in supporting Gag processing and infectivity, residue 37 is involved in the active site and residues 55, 57 and 59 in the flap in conferring the ability to specifically recognize HIV PR drugs. Ile37Val preserves tertiary structure but prevents steric clashes with the inhibitors. Asn55Met and Val59Ile induce a distinct kink in the flap and a new hydrogen bond to darunavir. Ile98Pro-Ser and Pro100Asn increase 90s loop flexibility, Gln99Val contributes hydrophobic contacts to the inhibitors, and Pro100Asn forms compensatory hydrogen bonds 717027
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4structure of enzyme-inhibitor complex with LP-149 647840
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4the two enzymes FIV protease and HIV-1 protease are strikingly similar at the crystallographic level, particularly within the substrate binding region 682966
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B4wild-type and mutant enzymes V59I and Q99V are cocrystallized with the C2-symmetric inhibitor TL-3, which contains (1S,2R,3R,4S)-1,4-diamino-1,4-dibenzyl-2,3-diol as the P1-P1' unit and Ala at P3/P3' positions 647832
Results 1 - 8 of 8