Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin

Maria A. Schumacher (), Andre F. Rivard, Hans Peter Bächinger and John P. Adelman
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Maria A. Schumacher: Vollum Institute, Oregon Health Sciences University
Andre F. Rivard: Vollum Institute, Oregon Health Sciences University
Hans Peter Bächinger: Shriners Hospital for Children, Research Unit
John P. Adelman: Vollum Institute, Oregon Health Sciences University

Nature, 2001, vol. 410, issue 6832, 1120-1124

Abstract: Abstract Small-conductance Ca2+-activated K+ channels (SK channels)1,2 are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming α-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the α-subunit immediately carboxy-terminal to the pore3,4. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM4. Here we report the 1.60 Å crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three α-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.

Date: 2001
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DOI: 10.1038/35074145

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