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Location of a ligand recognition site of FMRFamide‐gated Na + channels
Author(s) -
Cottrell G.A.,
Jeziorski M.C.,
Green K.A.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02081-6
Subject(s) - fmrfamide , xenopus , amiloride , helix (gastropod) , ligand gated ion channel , transmembrane domain , acid sensing ion channel , ion channel , chemistry , biophysics , biology , amino acid , microbiology and biotechnology , biochemistry , neuropeptide , receptor , sodium , gene , ecology , organic chemistry , snail
The second FMRFamide‐gated Na + channel ( Ht FaNaC), from Helisoma trivolvis , has been cloned. Ht FaNaC has some different pharmacological properties to Ha FaNaC, 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.