King's College London

Research portal

AFM imaging reveals the tetrameric structure of the TRPC1 channel

Research output: Contribution to journalArticle

N P Barrera, Y Shaifta, I McFadzean, J P T Ward, R M Henderson, J M Edwardson

Original languageEnglish
Pages (from-to)1086 - 1090
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - 13 Jul 2007

King's Authors


We have determined the subunit stoichiometry of the transient receptor potential C1 (TRPC1) channel by imaging isolated channels using atomic force microscopy (AFM). A frequency distribution of the molecular volumes of individual channel particles had two peaks, at 170 and 720 nm(3), corresponding with the expected sizes of TRPC1 monomers and tetramers, respectively. Complexes were formed between TRPC1 channels and antibodies against a V5 epitope tag present on each subunit. The frequency distribution of angles between pairs of bound antibodies had two peaks, at 88 degrees and 178 degrees. This result again indicates that the channel assembles as a tetramer. (C) 2007 Elsevier Inc. All rights reserved

View graph of relations

© 2018 King's College London | Strand | London WC2R 2LS | England | United Kingdom | Tel +44 (0)20 7836 5454