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The sigma-1 receptor (S1R) is a ligand-regulated membrane chaperone protein associated with endoplasmic reticulum stress response, and modulation of ion channel activities at the plasma membrane. We report here a solution NMR study of a S1R construct (S1R(Δ35)) in which only the first transmembrane domain and the eight-residue N-terminus have been removed. The second transmembrane helix is found to be composed of residues 91-107, which corresponds to the first steroid binding domain-like region. The cytosolic domain is found to contain three helices, and the secondary structure and backbone dynamics of the chaperone domain are consistent with that determined previously for the chaperone domain alone. The position of TM2 provides a framework for ongoing studies of S1R ligand binding and oligomerisation.

Original publication

DOI

10.1016/j.febslet.2015.01.033

Type

Journal article

Journal

FEBS Lett

Publication Date

27/02/2015

Volume

589

Pages

659 - 665

Keywords

NMR, Sigma-1 receptor, Transmembrane domain, Circular Dichroism, Humans, Magnetic Resonance Spectroscopy, Protein Structure, Secondary, Protein Structure, Tertiary, Receptors, sigma