Location of a ligand recognition site of FMRFamide‐gated Na+ channels

FEBS Letters

Green, K.A.¹  Jeziorski, M.C.²  Cottrell, G.A.¹ 

[1] School of Biology, Bute Medical Building, University of St. Andrews, Fife KY16 9TS, UK;Whitney Marine Laboratory, University of Florida, St. Augustine, FL 32086, USA

关键词: FaNaC;    FMRFamide recognition;    Amiloride;    Na+ channel;    Na+;    sodium ion;    FMRFamide;    Phe-Met-Arg-Phe-NH2;    PCR;    polymerase chain reaction;    TM;    transmembrane;    ENaC;    epithelial sodium channel;    ASIC;    acid-sensing ion channel;   

DOI  :  10.1016/S0014-5793(01)02081-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The second FMRFamide-gated Na⁺ channel (HtFaNaC), from Helisoma trivolvis, has been cloned. HtFaNaC has some different pharmacological properties to HaFaNaC, from Helix aspersa, which has enabled a rational approach to be made to start to identify the FMRFamide recognition site. Several chimeras were made by switching sections between the channels. The differences in sensitivity to FMRFamide, and amiloride, were assessed after expression in Xenopus oocytes. The data suggest that a recognition site for FMRFamide, and the potentiating action of amiloride, resides in a sequence of about 120 amino acids in the extracellular loop proximal to the first transmembrane segment.

【 授权许可】

Unknown