Abstract
Eukaryotic sodium and calcium channels are made up of four linked homologous but different transmembrane domains. Bacteria express sodium channels comprised of four identical subunits, each being analogous to a single homologous domain of their eukaryotic counterparts. Key elements of primary structure are conserved between bacterial and eukaryotic sodium and calcium channels. The simple protein structure of the bacterial channels has allowed extensive structure-function probes of key regions as well as allowing determination of several X-ray crystallographic structures of these channels. The structures have revealed novel features of sodium and calcium channel pores and elucidated the structural importance of many of the conserved features of primary sequence. The structural information has also formed the basis for computational studies probing the basis for sodium and calcium selectivity and gating.
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