Crystallization and preliminary X-ray crystallographic characterization of a cyclic nucleotide-binding homology domain from the mouse EAG potassium channel.

Maria João Marques-Carvalho, João Henrique Morais-Cabral

Acta crystallographica. Section F, Structural biology and crystallization communications 2012 Mar 01

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The members of the family of voltage-gated KCNH potassium channels play important roles in cardiac and neuronal repolarization, tumour proliferation and hormone secretion. These channels have a C-terminal cytoplasmic domain which is homologous to cyclic nucleotide-binding domains (CNB-homology domains), but it has been demonstrated that channel function is not affected by cyclic nucleotides and that the domain does not bind nucleotides in vitro. Here, the crystallization and preliminary crystallographic analysis of a CNB-homology domain from a member of the KCNH family, the mouse EAG channel, is reported. X-ray diffraction data were collected to 2.2 Å resolution and the crystal belonged to the hexagonal space group P3(1)21. © 2012 International Union of Crystallography

Citation

Maria João Marques-Carvalho, João Henrique Morais-Cabral. Crystallization and preliminary X-ray crystallographic characterization of a cyclic nucleotide-binding homology domain from the mouse EAG potassium channel. Acta crystallographica. Section F, Structural biology and crystallization communications. 2012 Mar 01;68(Pt 3):337-9