Basso C, Labarca P, Stefani E, Alvarez O, Latorre R
Departmento of Biología, Facultad de Ciencias, Universidad de Chile, Santiago.
FEBS Lett. 1998 Jun 16;429(3):375-80. doi: 10.1016/s0014-5793(98)00635-8.
Shaker K+ channels inactivate through two distinct molecular mechanisms: N-type, which involves the N-terminal domain and C-type that appears to involve structural modifications at the external mouth of the channel. We have tested pore accessibility of the Shaker K+ channel during C-type inactivation using Ba2+ as a probe. We determined that external Ba2+ binds to C-type inactivated channels forming an extremely stable complex; i.e. there is Ba2+ trapping by C-type inactivated channels. The structural changes Shaker channels undergo during C-type inactivation create high energy barriers that hinder Ba2+ exit to either the extracellular solution or to the intracellular solution.
Shaker钾通道通过两种不同的分子机制失活:N型,涉及N端结构域;C型,似乎涉及通道外口的结构修饰。我们使用Ba2+作为探针,测试了C型失活期间Shaker钾通道的孔可及性。我们确定外部Ba2+与C型失活通道结合形成极其稳定的复合物;即C型失活通道存在Ba2+捕获现象。Shaker通道在C型失活过程中发生的结构变化产生了高能垒,阻碍Ba2+向细胞外溶液或细胞内溶液中逸出。