Conformational dynamics of CYP3A4 demonstrate the important role of Arg212 coupled with the opening of ingress, egress and solvent channels to dehydrogenation of 4-hydroxy-tamoxifen

Structure-based methods for P450 substrates are commonly used during drug development to identify sites of metabolism. However, docking studies using available X-ray structures for the major drug-metabolizing P450, CYP3A4, do not always identify binding modes supportive of the production of high-ene...

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Vydáno v:	Biochimica et biophysica acta Ročník 1820; číslo 10; s. 1605 - 1617
Hlavní autoři:	Shahrokh, Kiumars, Cheatham, Thomas E., Yost, Garold S.
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Netherlands Elsevier B.V 01.10.2012
Témata:	4-Hydroxy‐tamoxifen active sites Arginine - genetics Arginine - physiology Conformational dynamics Cytochrome P-450 CYP3A - chemistry Cytochrome P-450 CYP3A - genetics Cytochrome P-450 CYP3A - metabolism Cytochrome P-450 CYP3A - physiology Dehydrogenation Docking drugs enzymes gases heme Humans Hydrogenation hydroxylation Ion Channel Gating - genetics Ion Channel Gating - physiology liquid chromatography metabolism metabolites Models, Biological Models, Molecular Molecular Docking Simulation Molecular dynamics Molecular Dynamics Simulation Mutagenesis, Site-Directed P450 Protein Binding Protein Conformation Protein Interaction Domains and Motifs - genetics Protein Interaction Domains and Motifs - physiology risk site-directed mutagenesis solvents Solvents - metabolism spectroscopy structures Tamoxifen - analogs & derivatives Tamoxifen - chemistry Tamoxifen - metabolism Tamoxifen - pharmacokinetics toxicity X-radiation SOM Dehydrogenation Conformational dynamics Molecular dynamics Docking P450 4-Hydroxy‐tamoxifen RALX 4OHT
ISSN:	0304-4165, 0006-3002, 1872-8006
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