Castillo, Juan P.Sánchez-Rodríguez, Jorge E.Hyde, H. ClarkZaelzer, Cristian A.Aguayo, DanielSepúlveda, Romina V.Luk, Louis Y.P.Kent, Stephen B.H.Gonzalez-Nilo, Fernando D.Bezanilla, FranciscoLatorre, Ramón2023-10-252023-10-252016-06Proceedings of the National Academy of Sciences of the United States of America. Volume 113, Issue 23, Pages E3231 - E3239. 7 June 20160027-8424https://repositorio.unab.cl/xmlui/handle/ria/53625Indexación: Scopus.Large-conductance Ca2+- and voltage-activated K+ (BK) channels are involved in a large variety of physiological processes. Regulatory β-subunits are one of the mechanisms responsible for creating BK channel diversity fundamental to the adequate function of many tissues. However, little is known about the structure of its voltage sensor domain. Here, we present the external architectural details of BK channels using lanthanide-based resonance energy transfer (LRET). We used a genetically encoded lanthanide-binding tag (LBT) to bind terbium as a LRET donor and a fluorophore-labeled iberiotoxin as the LRET acceptor for measurements of distances within the BK channel structure in a living cell. By introducing LBTs in the extracellular region of the α- or β1-subunit, we determined (i) a basic extracellular map of the BK channel, (ii) β1-subunit–induced rearrangements of the voltage sensor in α-subunits, and (iii) the relative position of the β1-subunit within the α/β1-subunit complex.enLanthanide Resonance Energy TransferBK Channelsβ1-subunitArtículo10.1073/pnas.1606381113