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学科主题: 生命有机化学
题名: Interaction sites between the Slo1 pore and the NH2 terminus of the beta(2) subunit, probed with a three-residue sensor
其他题名: 用三残基探针探测钾离子通道Slo1孔道与第二亚单元NH2末端相互作用位点
作者: Li H(李辉) ; Yao J(姚镜) ; Tong XT(童孝田) ; Guo ZH(郭兆华) ; Wu Y(吴英) ; Sun L(孙亮) ; Pan N(潘娜) ; Wu HM(吴厚铭) ; Xu T(徐滔) ; Ding JP(丁久平)
通讯作者: 丁久平
刊名: J. Biol. Chem.
发表日期: 2007
卷: 282, 期:24, 页:17720-17728
收录类别: SCI
部门归属: 华中科技大学; 上海有机所
英文摘要: Calcium- and voltage-gated (BK) K+ channels encoded by Slo1 play an essential role in nervous systems. Although it shares many common features with voltage-dependent KV channels, the BK channel exhibits differences in gating and inactivation. Using a mutant in which FWI replaces three residues (FIW) in the NH2 terminus of wild-type beta 2-subunits, in conjunction with alanine-scanning mutagenesis of the Slo1 S6 segment, we identify that the NH2 terminus of beta 2-subunits interacts with the residues near the cytosolic superficial mouth of BK channels during inactivation. The cytosolic blockers did not share the sites with NH2 terminus of beta 2-subunits. A novel blocking-inactivating scheme was proposed to account for the observed noncompetition inactivation. Our results also suggest that the residue Ile-323 plays a dual role in interacting with the NH2 terminus of beta 2-subunits and modulating the gating of BK channels.
语种: 英语
相关网址: 查看原文
WOS记录号: WOS:000247084500045
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/17381
Appears in Collections:上海有机化学研究所_期刊论文

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Recommended Citation:
Li H,Yao J,Tong XT,et al. Interaction sites between the Slo1 pore and the NH2 terminus of the beta(2) subunit, probed with a three-residue sensor[J]. J. Biol. Chem.,2007,282(24):17720-17728.
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