首页|Structural modeling of Nav1.5 pore domain in closed state
Structural modeling of Nav1.5 pore domain in closed state
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The voltage-dependent cardiac sodium channel plays a key role in cardiac excitability and conduction and it is the drug target of medically important.However,its atomic-resolution structure is still lack.Here,we report a modeled structure of Nav1.5 pore domain in closed state.The structure was con-structed by Rosetta-membrane homology modeling method based on the template of eukaryotic Nav channel NavPaS and selected by energy and direct coupling analysis (DCA).Moreover,this structure was optimized through molecular dynamical simulation in the lipid membrane bilayer.Finally,to vali-date the constructed model,the binding energy and binding sites of closed-state local anesthetics (LAs)in the modeled structure were computed by the MM-GBSA method and the results are in agreement with experiments.The modeled structure of Nav1.5 pore domain in closed state may be useful to ex-plore molecular mechanism of a state-dependent drug binding and helpful for new drug development.
Nav1.5 ion channelClosed stateHomology modelingDirect coupling analysisLocal anestheticsDrug binding
Xiaofeng Ji、Yanzhao Huang、Jun Sheng
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Yellow Sea Fisheries Research Institute,Chinese Academy of Fishery Sciences,Qingdao 266071,Shandong,China
School of Physics,Huazhong University of Science and Technology,Wuhan 430074,China
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