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- W2365680010 abstract "To study the impact of ouabain on the conformation change of Na+,K+-ATPase,a new method based on molecular dynamics simulation was proposed. Firstly,complex can be obtained through docking,then,simulate enzyme monomer and its compounds in the same environment. The results showed that after ouabain binding to Na+,K+-ATPase,αM1 and αM2 of Na+,K+-ATPase move toward to ouabain and the A domain is slightly moving toward to P domain in the E2P: ouabain form; and Hydrophobic residues Phe783,Thr797,Val322,Gly319,Ile320,Ile321,Leu125,Ile315,Ala112 in binding pocket form hydrophobic effect with ouabain and polar residues,Asp121,Thr797,Gln111 form hydrogen bonds with ouabain. Comparison of the E2P: ouabain complex with E2P structure,in E2P: ouabain complex,212TGES215loop of A domain and flanking residues bury the phosphorylated Asp369 residue,protecting it against spontaneous hydrolysis. This prevents E1and E2 conformational change necessary for the function of the protein,then inhibit the activity of enzyme and stimulate the calcium ion mediated signaling channel. The method proposed in the paper not only intuitively shows the conformational changes of Na+,K+-ATPase,but well explains the mechanism of interaction of ouabain and Na+,K+-ATPase,and those data play a guiding role for further study." @default.
- W2365680010 created "2016-06-24" @default.
- W2365680010 creator A5073284766 @default.
- W2365680010 date "2014-01-01" @default.
- W2365680010 modified "2023-09-28" @default.
- W2365680010 title "Molecular Dynamics Simulation of Impact of Na,K-ATPase Conformation Combined with Ouabain" @default.
- W2365680010 hasPublicationYear "2014" @default.
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