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. 2019 Sep 20;10:972. doi: 10.3389/fphar.2019.00972

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Copyright © 2019 Shim, Brown, Singh, Singh, Fettinger, Yarov-Yarovoy and Wulff

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Interactions between SKA-111 and residues in the K_Ca3.1 S₄₅A helix (A) and the CaM N-lobe (B) interface pocket. Hydrogen bonds are indicated by black lines, van der Waals interactions are indicated by purple lines. (C) The K_Ca3.1-CaM channel complex seen from the intracellular side. The S₄₅A helix/CaM N-lobe interface colored dark blue. Two other, potential binding sites for small molecules are highlighted with orange or sky-blue circles. The channel is shown in gray, the CaM C-lobe in purple and the CaM N-lobe in yellow.