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Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor

Ortega-Roldan, Jose L., Ossa, Felipe, Amin, Nader T., Schnell, Jason R. (2015) Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor. FEBS Letters, 589 (5). pp. 659-665. ISSN 0014-5793. (doi:10.1016/j.febslet.2015.01.033)

Abstract

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(?35)) 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.

Item Type: Article
DOI/Identification number: 10.1016/j.febslet.2015.01.033
Subjects: Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Jose Ortega-Roldan
Date Deposited: 13 Nov 2016 22:35 UTC
Last Modified: 06 Feb 2020 14:57 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/58599 (The current URI for this page, for reference purposes)
Ortega-Roldan, Jose L.: https://orcid.org/0000-0002-6316-4390
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