. . . . . "Anzenbacherov\u00E1, Eva" . . "Lessons from known P450 structures" . . "Zn\u00E1m\u00E9 struktury cytochromu P450"@cs . . "0232-0061" . "Lessons from known P450 structures"@en . "[802A7AC10D3C]" . "43" . "198" . "Anzenbacher, Pavel" . "571404" . . . . . "Lessons from known P450 structures" . . "RIV/61989592:15310/04:00002037!RIV/2005/GA0/153105/N" . "P(GA203/99/0277), Z(MSM 153100007)" . "cytochromes;cytochrome P450;structures"@en . "CZ - \u010Cesk\u00E1 republika" . . "Lessons from known P450 structures"@en . "\u010Cl\u00E1nek se zab\u00FDv\u00E1 zn\u00E1m\u00FDmi strukturami cytochromu P450."@cs . . "There is a considerable progress last five years in knowledge of the P450 (CYP) structures which allows to draw out at least some conclusions important for function of the respective enzymes. First, the structure of mammalian (rabbit) liver microsomal CYP2C5 was published in 2000 which allowed for detailed comparisons of all important human liver microsomal P450s. The next milestone was the structure of CYP2C9 presented in full in 2003 showing the first human liver microsomal P450 in the absence as well as in the presence of substrate. Third success was the resolution of the CYP3A4 structure presented this year. The structures show that although the overall %22P450 fold%22 is preserved, there are considerable differences in the ways the substrates approach the active site and in the properties of the active site itself. Relative flexibility and openness of the CYP3A4 active site was expected by the modeling as well as by the spectroscopic approaches. The CYP2C9 structure opens a possibility to study in mo" . "3"^^ . "Suppl." . "15310" . "Zn\u00E1m\u00E9 struktury cytochromu P450"@cs . "Otyepka, Michal" . . "There is a considerable progress last five years in knowledge of the P450 (CYP) structures which allows to draw out at least some conclusions important for function of the respective enzymes. First, the structure of mammalian (rabbit) liver microsomal CYP2C5 was published in 2000 which allowed for detailed comparisons of all important human liver microsomal P450s. The next milestone was the structure of CYP2C9 presented in full in 2003 showing the first human liver microsomal P450 in the absence as well as in the presence of substrate. Third success was the resolution of the CYP3A4 structure presented this year. The structures show that although the overall %22P450 fold%22 is preserved, there are considerable differences in the ways the substrates approach the active site and in the properties of the active site itself. Relative flexibility and openness of the CYP3A4 active site was expected by the modeling as well as by the spectroscopic approaches. The CYP2C9 structure opens a possibility to study in mo"@en . "Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica" . "3"^^ . "RIV/61989592:15310/04:00002037" . . . "275"^^ . .