Structural basis of allosteric interactions among Ca2+-binding sites in a K+ channel RCK domain

Frank J. Smith, Victor P.T. Pau, Gino Cingolani and Brad S. Rothberg ()
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Frank J. Smith: Temple University School of Medicine
Victor P.T. Pau: Temple University School of Medicine
Gino Cingolani: Thomas Jefferson University
Brad S. Rothberg: Temple University School of Medicine

Nature Communications, 2013, vol. 4, issue 1, 1-10

Abstract: Abstract Ligand binding sites within proteins can interact by allosteric mechanisms to modulate binding affinities and control protein function. Here we present crystal structures of the regulator of K+ conductance (RCK) domain from a K+ channel, MthK, which reveal the structural basis of allosteric coupling between two Ca2+ regulatory sites within the domain. Comparison of RCK domain crystal structures in a range of conformations and with different numbers of regulatory Ca2+ ions bound, combined with complementary electrophysiological analysis of channel gating, suggests chemical interactions that are important for modulation of ligand binding and subsequent channel opening.

Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3621

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DOI: 10.1038/ncomms3621

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