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

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(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 regi...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More from this funder
Name:
Medical Research Council
Grant:
K018590
Publisher:
Elsevier
Journal:
FEBS Letters More from this journal
Volume:
589
Issue:
5
Pages:
659-665
Publication date:
2015-02-01
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
Language:
English
Keywords:
Pubs id:
pubs:506712
UUID:
uuid:1c691eb9-d7a6-49f5-a83d-9efbed338314
Local pid:
pubs:506712
Source identifiers:
506712
Deposit date:
2015-04-29

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