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Modeling

Structural Model of the Ca_V1.2 Pore

Anna Stary, Yinon Shafrir, Steffen Hering, Peter Wolschann and H. Robert Guy

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Understanding the structure and functional mechanisms of voltage-gated calcium channels remains a major task in membrane biophysics. In the absence of three dimensional structures, homology modelling techniques are the method of choice, to address questions concerning the structure of these channels. We have developed models of the open Cav1.2 pore, based on the crystal structure of the mammalian voltage-gated potassium channel Kv1.2 and a model of the bacterial sodium channel NaChBac. Our models are developed to be consistent with experimental data and modelling criteria. The models highlight major differences between voltage-gated potassium and calcium channels, in the P segments, as well as the inner pore helices. Molecular dynamics simulations support the hypothesis of a clockwise domain arrangement and experimental observations of asymmetric calcium channel behaviour. In the accompanying paper these models were used to study structural effects of a channelopathy mutation.

Authors

Anna Stary

Max Planck Institute for Biophysical Chemistry

Yinon Shafrir

NCI, NIH

Steffen Hering

University of Vienna

Peter Wolschann

Institute for Theoretical Chemistry

H. Robert Guy

NIH

This is an open-access article

 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.