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- W2014363759 abstract "In continuation of our previous work (Stary et al. 2007, Beyl et al. 2010) we have analyzed the functional role of gating determinants in the bundle crossing region of Cav1.2. G432 (IS6), A780 (IIS6), G1193 (previous data, IIIS6) and A1503 (IVS6) were substituted with residues of different physicochemical properties. This ‘G/A/G/A’ motif was identified in a conservation analysis showing that Cav, Nav, TRP and many K channels contain glycines or alanines in equivalent positions. Most ‘G/A/G/A’ mutations shifted the activation curve in the hyperpolarizing direction, suggesting a destabilization of the closed and a stabilization of the open channel state. Mutations G432A/V, G1193A and A1503V did, however, stabilize the closed channel conformation as evident from rightward shifts of the activation curves. A comparison with the closed KcsA structure revealed that the ‘G/A/G/A’ motif (‘A/A/A/A’ in KcsA) is located at the narrowest point of the interface between two S6 (M2) helices, tightly packed in a hydrophobic environment. Our analysis suggests that size and hydrophobicity might be important for channel gating. We found that mutations to methionine or tryptophan either destabilize the closed channel or result in non-conducting channels. Small hydrophobic residues like alanine or valine stabilize the resting state. A comparison between resting and open state KcsA structures indicates that the ‘G/A/G/A’ motif and surrounding residues in Cav1.2 undergo large conformational changes upon gating, resulting in a displacement of more than 7 Å. 1 Stary, A., Shafrir, Y., Hering, S., Wolschann, P., Guy, H.R. (2007) Channels 2(3), 210-215. 2 Beyl, S., Depil, K., Hohaus, A., Stary-Weinzinger, A., Timin, E., Shabbir, W., Kudrnac, M., Hering, S. (2010) Pflugers Arch, in press." @default.
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- W2014363759 date "2011-02-01" @default.
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- W2014363759 title "Mutational Analysis in the Bundle Crossing Region Guides the Design of Cav1.2 Homology Models" @default.
- W2014363759 doi "https://doi.org/10.1016/j.bpj.2010.12.3298" @default.
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