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Solution NMR studies reveal the location of the second transmembrane domain of the human sigma‐1 receptor
Author(s) -
Ortega-Roldan Jose Luis,
Ossa Felipe,
Amin Nader T.,
Schnell Jason R.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.01.033
Subject(s) - transmembrane domain , sigma 1 receptor , transmembrane protein , chaperone (clinical) , chemistry , endoplasmic reticulum , biophysics , helix (gastropod) , nuclear magnetic resonance spectroscopy , stereochemistry , membrane , biochemistry , receptor , biology , medicine , ecology , pathology , snail , agonist
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.