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Structural basis of the SK Potassium Channel Controlling the Selectivity of Recognition by Scorpion Toxins

Structural basis of the SK Potassium Channel Controlling the...

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第十一届中国生物毒素研究及医药应用年会

作者： Jing Feng Youtian Hu Hong Yi Shijin Yin Song Han Jun Hu Zongyun Chen Weishan Yang Zhijian Cao Michel De Waard Jean-Marc Sabatier Wenxin Li 吴英亮 State Key Laboratory of Virology College of Life SciencesWuhan University Inserm U836 Grenoble Neuroscience InstituteLaboratory of Excellence 'Ion Channels Science and Therapeutics 'Universit Joseph FourierBtiment Edmond Safra38042 Grenoble Cedex 09France Inserm UMR1097 Aix-Marseille UniversiteParc Scientifique de Luminy13288 MarseilleFrance 武汉大学生命科学学院湖北省武汉市武汉大学生命科学学院

Potassium channel functions are often deciphered by using selective and potent scorpion *** these toxins,only a limited subset is capable to selectively block small conductance Ca-activated K(SK) *** sequence alignment,we found that SK channel turret residues are highly *** there are also some additional basic residues on the turret when compared with other potassium *** we presumed that there should be uniform structure bases of this selective SK channel *** this work, SK3 channel is exampled to demonstrate the key role of the electric charges of two conserved arginine residues(R485 and R489) from the SK3 channel outer vestibule in the selective recognition by SK3-blocking BmP05 ***,individually substituting these residues by histidyl or lysyl(maintaining partially or fully the positive electric charge),while decreasing the affinity of BmP05,still preserves its toxin-sensitivity profile(as evidenced by the lack of recognition by many other potassium channel-sensitive charybdotoxin(ChTX)).In contrast, when R485 or R489 residue of SK3 channel is mutated towards an acidic(E) or alcoholic(S) amino acid residue,the channel loses its sensitivity to BmP05 and becomes susceptible to a ’new’ blocking activity by *** these basic SK3 channel residues important for sensitivity,two acidic D492 and D518 residues,also located in the SK3 channel outer vestibule,were identified as being critical for toxin ***,molecular modeling data indicate the existence of a compact SK3 channel turret conformation,like a peptide screener, where the basic rings of R485 and R489 residues are stabilized by strong ionic interactions with D492 and D518 *** conclusion,the unique properties of two conserved arginine residues(spatial orientations and molecular interactions) of SK channel account for its toxin-sensitivity profile.

关键词： Scorpion toxin recognition control conserved arginine residue SK3 channel outer vestibule electrostatic repulsion forces

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