“NMR structure and dynamics of a designed water-soluble transmembrane domain of nicotinic acetylcholine receptor,” by Tanxing Cui, David Mowrey, Vasyl Bondarenko, Tommy Tillman, Dejian Ma, Elizabeth Landrum, Jose Manuel Perez-Aguilar, Jing He, Wei Wang, Jeffery G. Saven, Roderic G. Eckenhoff, Pei Tang, and Yan Xu, was published as the cover story in the March issue of Biochimica et Biophysica Acta (BBA) Biomembranes.
In their paper, the authors report their computational design and experimental characterization of WSA, a water-soluble protein nearly similar to the transmembrane domain of the nicotinic acetylcholine receptor (nAChR) α1 subunit. nAChR is an important therapeutic target for a wide range of pathophysiological conditions, for which rational drug designs often require receptor structures at atomic resolution. Their results illustrate the usefulness of high-resolution NMR analyses of water-solubilized channel proteins for the discovery of potential drug binding sites.