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Titolo:
Molecular modelling of CYP2B6, the human CYP2B isoform, by homology with the substrate-bound CYP102 crystal structure: evaluation of CYP2B6 substratecharacteristics, the cytochrome b(5) binding site and comparisons with CYP2B1 and CYP2B4
Autore:
Lewis, DFV; Lake, BG; Dickins, M; Eddershaw, PJ; Tarbit, MH; Goldfarb, PS;
Indirizzi:
Univandrrey, Sch Biol Sci, Mol Toxicol Grp, Guildford GU2 5XH, Surrey, Engl Univ Surrey Guildford Surrey England GU2 5XH ldford GU2 5XH, Surrey, Engl BIBRA Int, Carshalton SM5 4DS, Surrey, England BIBRA Int Carshalton Surrey England SM5 4DS lton SM5 4DS, Surrey, England Glaxo Wellcome Res & Dev Ltd, Ware SG12 0DP, Herts, England Glaxo WellcomeRes & Dev Ltd Ware Herts England SG12 0DP , Herts, England
Titolo Testata:
XENOBIOTICA
fascicolo: 4, volume: 29, anno: 1999,
pagine: 361 - 393
SICI:
0049-8254(199904)29:4<361:MMOCTH>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHENYL-IRON COMPLEXES; LIVER MICROSOMAL CYTOCHROME-P-450; AMINO-ACID-RESIDUES; DIRECTED MUTAGENESIS; ACTIVE-SITE; INSITU REARRANGEMENT; RECOGNITION SITES; BENZPHETAMINE ANALOGS; TOPOLOGICAL ANALYSIS; STEROID-METABOLISM;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
106
Recensione:
Indirizzi per estratti:
Indirizzo: Lewis, DFV Univandrrey, Sch Biol Sci, Mol Toxicol Grp, Guildford GU2 5XH, Surrey, Engl Univ Surrey Guildford Surrey England GU2 5XH 5XH, Surrey, Engl
Citazione:
D.F.V. Lewis et al., "Molecular modelling of CYP2B6, the human CYP2B isoform, by homology with the substrate-bound CYP102 crystal structure: evaluation of CYP2B6 substratecharacteristics, the cytochrome b(5) binding site and comparisons with CYP2B1 and CYP2B4", XENOBIOTICA, 29(4), 1999, pp. 361-393

Abstract

1. Molecular modelling studies of CYP2B isoforms from rat (CYP2B1), rabbit(CYP2B4) and man (CYP2B6) are reported, with particular emphasis on substrate interactions with the human CYP2B isoform, CYP2B6.2. The findings represent an advance on our previous study that focused primarily on the rat CYP2B isoform, CYP2B1, and involved homology modelling with substrate-free CYP102.3. The current work utilizes the recently published substrate-bound CYP102crystal structure as a template for construction of the CYP2B subfamily isoforms and shows, in particular, that known CYP2B6 substrate specificity and regioselectivity can be rationalized by putative active site interactions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 12:21:22