Molecular modelling of CYP2B6, the human CYP2B isoform, by homology with the substrate-bound CYP102 crystal structure: evaluation of CYP2B6 substrate characteristics, the cytochrome b5 binding site and comparisons with CYP2B1 and CYP2B4.
Xenobiotica
; 29(4): 361-93, 1999 Apr.
Article
de En
| MEDLINE
| ID: mdl-10375007
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 CYP102 crystal 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.
Recherche sur Google
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Oxidoreductases, (N-demethylating)
/
Steroid hydroxylases
/
Protéines bactériennes
/
Aryl hydrocarbon hydroxylases
/
Modèles moléculaires
/
Cristallographie aux rayons X
/
Cytochrome P-450 CYP2B1
/
Cytochrome P-450 enzyme system
/
Mixed function oxygenases
/
L-Lactate dehydrogenase
Type d'étude:
Prognostic_studies
Limites:
Animals
/
Humans
Langue:
En
Journal:
Xenobiotica
Année:
1999
Type de document:
Article
Pays d'affiliation:
Royaume-Uni