Improved cytochrome P450 3A4 molecular models accurately predict the Phe215 requirement for raloxifene dehydrogenation selectivity

Biochemistry

Volumn 49, Issue 41, 2010, Pages 9011-9019

  Moore, Chad D ^a   Shahrokh, Kiumars ^a   Sontum, Stephen F ^b   Cheatham, Thomas E ^a   Yost, Garold S ^a  

^a UNIVERSITY OF UTAH   (United States)

^b MIDDLEBURY COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; DEHYDROGENATION; DOCKING; ENZYMES; FORECASTING; METABOLISM; MODEL STRUCTURES; MOLECULAR MODELING; MOLECULAR ORIENTATION; MUTAGENESIS; OXYGENATION; PORPHYRINS;

ACTIVE SITE; ACTIVE SITE RESIDUES; AUTODOCK; CATALYTIC MECHANISMS; CYTOCHROME P450; CYTOCHROME P450-3A4; DEHYDROGENATION SELECTIVITY; ENZYME MODELS; ENZYME-SUBSTRATE INTERACTIONS; HEME MOIETY; IMPROVED MODELS; LIGAND DOCKING; MOLECULAR MODELS; PARTIAL CHARGES; PROTEIN DATA BANK; PROTEIN-BINDING; SELECTIVE DEHYDROGENATIONS; SITE DIRECTED MUTAGENESIS; STATIC MODEL; STERIC INTERACTIONS; STRUCTURAL MODELS; SUBSTRATE ORIENTATION;

SUBSTRATES;

CYTOCHROME P450 3A4; GLUTAMINE; GLYCINE; PHENYLALANINE; RALOXIFENE; CYP3A4 PROTEIN, HUMAN; CYTOCHROME P450 3A; HEME; PROTEIN BINDING;

ACCURACY; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DEHYDROGENATION; ENZYME SUBSTRATE COMPLEX; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MOLECULAR DOCKING; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DATA BANK; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY; AMINO ACID SUBSTITUTION; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; GENETICS; HUMAN; METABOLISM; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 CYP3A; ENZYME ACTIVATION; HEME; HUMANS; MODELS, MOLECULAR; PHENYLALANINE; PROTEIN BINDING; RALOXIFENE;

EID: 77957898647     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101139q     Document Type: Article

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