- 著者
 
          - 
             
             下村 拓史
             
             入江 克雅
             
          
 
          
          
          - 出版者
 
          - 一般社団法人 日本生物物理学会
 
          
          
          - 雑誌
 
          - 生物物理 (ISSN:05824052)
 
          
          
          - 巻号頁・発行日
 
          - vol.61, no.4, pp.223-226, 2021 (Released:2021-07-30)
 
          
          
          - 参考文献数
 
          - 10
 
          
          
        
        
        
        Voltage-dependent Ca2+ channels (Cavs) are indispensable for coupling action          potentials with Ca2+ signaling. We report the first identification of a native          prokaryotic Cav, CavMr, whose selectivity filter contains a smaller number of negatively          charged residues than that of artificial prokaryotic Cavs. A relative mutant whose          selectivity filter was replaced with that of CavMr exhibits high Ca2+          selectivity. The glycine residue of the CavMr selectivity filter is a determinant for            Ca2+ selectivity. This glycine residue is well conserved among subdomains I          and III of eukaryotic Cavs, which provide new insight into Ca2+ selectivity          mechanism conserved from prokaryotes to eukaryotes.