来自蝎毒素分子表面完整功能图谱的钾离子通道结构暗示

Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin.

作者信息

Stampe P, Kolmakova-Partensky L, Miller C

机构信息

Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254-9110.

出版信息

Biochemistry. 1994 Jan 18;33(2):443-50. doi: 10.1021/bi00168a008.

DOI:10.1021/bi00168a008

PMID:7506933

Abstract

The external vestibules of many K+ channels carry a high-affinity receptor for charybdotoxin, a peptide of known structure. Point mutations of a recombinant toxin identified the residues directly involved in the interaction with a Ca(2+)-activated K+ channel. The interaction surface is formed from 8 of the 37 residues and covers about 25% of the peptide's molecular surface. The shape of the toxin permits a deduced picture of the complementary receptor site in the external vestibule of the K+ channel.

摘要

许多钾离子通道的外部前庭带有对已知结构的肽——蝎毒素的高亲和力受体。重组毒素的点突变确定了与钙激活钾离子通道相互作用直接相关的残基。相互作用表面由37个残基中的8个形成，覆盖了该肽分子表面约25%的面积。毒素的形状使我们能够推断出钾离子通道外部前庭中互补受体位点的情况。