title: AFM imaging reveals the tetrameric structure of the TRPC1 channel.
abstract: 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.
authors.affiliation: Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK.
authors.forename: Nelson P
authors.initials: NP
authors.lastname: Barrera
authors.forename: Yasin
authors.initials: Y
authors.lastname: Shaifta
authors.forename: Ian
authors.initials: I
authors.lastname: McFadzean
authors.forename: Jeremy P T
authors.initials: JP
authors.lastname: Ward
authors.forename: Robert M
authors.initials: RM
authors.lastname: Henderson
authors.forename: J Michael
authors.initials: JM
authors.lastname: Edwardson
mesh_terms: D019281:Dimerization; D018625:Microscopy, Atomic Force; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011487:Protein Conformation; D050052:TRPC Cation Channels / Q000648:ultrastructure*
chemical_list: D046912:Multiprotein Complexes; D050052:TRPC Cation Channels; C096351:transient receptor potential cation channel, subfamily C, member 1