Open AccessCrystallization and preliminary X‐ray crystallographic characterization of a cyclic nucleotide‐binding homology domain from the mouse EAG potassium channel
Author(s) -
MarquesCarvalho Maria João,
MoraisCabral João Henrique
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112004216
Subject(s) - nucleotide , potassium channel , cyclic nucleotide binding domain , crystallization , crystallography , homology (biology) , chemistry , homology modeling , biophysics , amino acid , biology , biochemistry , gene , organic chemistry , enzyme
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 P 3 1 21.