Homology modeling, binding site identification and docking in flavone hydroxylase CYP105P2 in Streptomyces peucetius ATCC 27952
Homology modeling, binding site identification and docking in flavone hydroxylase CYP105P2 in Streptomyces peucetius ATCC 27952
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DOI：
10.1016/j.compbiolchem.2010.08.002
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发表时间：
2010-08-01
影响因子：
3.1
通讯作者：
Sohng, Jae Kyung
中科院分区：
文献类型：
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作者：
Kanth, Bashistha Kumar;Liou, Kwangkyoung;Sohng, Jae Kyung
细胞色素P450 105P2的同源性模型使用四种P450结构CYP105A1、CYP105、CYP165B3和CYP107L1作为用于模型构建的模板来构建CYP105P2（CYP105P2）。链环境通过分子动力学对使用这些模板构建的CYP 105 P2模型进行进一步的活性位点优化，以生成最终的CYP 105 P2模型。将底物黄酮、黄烷酮、槲皮素和柚皮素对接到模型中。黄酮复合物用于验证活性位点结构，并通过随后的二级结构表征鉴定结构和功能上重要的残基（C）2010 Elsevier Ltd保留所有权利
Homology models of cytochrome P450 105P2 (CYP105P2) were constructed using four P450 structures CYP105A1 CYP105 CYP165B3 and CYP107L1 as templates for the model building Using Accelrys Discovery Studio 2 1 software the lowest energy CYP105P2 model was then assessed for stereochemical quality and side-chain environment Further active site optimization of the CYP105P2 model built using these templates was performed by molecular dynamics to generate the final CYP105P2 model The substrates flavone flavanone quercetin and naringenin were docked into the model The model-flavone complex was used to validate the active site architecture and structurally and functionally important residues were identified by subsequent characterization of the secondary structure (C) 2010 Elsevier Ltd All rights reserved