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Structural modeling of human cardiac sodium channel pore domain

文献类型： 外文期刊

作者： Ji, Xiaofeng 1 ; Xiao, Yi 1 ; Liu, Shiyong 1 ;

作者机构： 1.Huazhong Univ Sci & Technol, Sch Phys, Wuhan 430074, Hubei, Peoples R China

2.Huazhong Univ Sci & Technol, Minist Educ, Key Lab Mol Biophys, Wuhan 430074, Hubei, Peoples R China

3.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Shandong, Peoples R China

关键词： Na(v)1; 5 pore domain; three-dimensional structure; homology modeling; binding sites; local anesthetic drugs

期刊名称：JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS （ 影响因子：3.31； 五年影响因子：2.689 ）

ISSN： 0739-1102

年卷期： 2018 年 36 卷 9 期

页码：

收录情况： SCI

摘要： The pore domain of human voltage-dependent cardiac sodium channel Na(v)1.5 (hNa(v)1.5) is the crucial binding targets for anti-arrhythmics drugs and some local anesthetic drugs but its three-dimensional structure is still lacking. This has affected the detailed studies of the binding features and mechanism of these drugs. In this paper, we present a structural model for open-state pore domain of hNa(v)1.5 built using single template ROSETTA-membrane homology modeling with the crystal structure of NavMs. The assembled structural models are evaluated by rosettaMP energy and locations of binding sites. The modeled structures of the pore domain of hNa(v)1.5 in open state will be helpful to explore molecular mechanism of a state-dependent drug binding and help designing new drugs.

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