Related ArticlesSolution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.
FEBS Lett. 2015 Jan 31;
Authors: Ortega-Roldan JL, Ossa F, Amin NT, Schnell JR
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.
PMID: 25647032 [PubMed - as supplied by publisher]
[NMR paper] Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
FEBS Lett. 2014 Nov 3;588(21):3802-7
Authors: Mineev KS, Goncharuk SA, Arseniev AS
Abstract
Toll-like receptors (TLRs) take part in both the innate and...
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[NMR paper] Expression, purification and reconstitution of the C-terminal transmembrane domain of scavenger receptor BI into detergent micelles for NMR analysis.
Expression, purification and reconstitution of the C-terminal transmembrane domain of scavenger receptor BI into detergent micelles for NMR analysis.
Expression, purification and reconstitution of the C-terminal transmembrane domain of scavenger receptor BI into detergent micelles for NMR analysis.
Protein Expr Purif. 2014 Nov 12;
Authors: Chadwick AC, Jensen DR, Peterson FC, Volkman BF, Sahoo D
Abstract
Scavenger receptor class B type I (SR-BI), the high density lipoprotein (HDL) receptor, is important for the delivery of...
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12-03-2014 04:05 PM
[NMR paper] Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B.
Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B.
Related Articles Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B.
Proteins. 2014 Apr 17;
Authors: Lund G, Cierpicki T
Abstract
The CDC25B phosphatase is a critical regulator of the cell cycle and has been validated as an important therapeutic target in cancer. Previous studies using molecular dynamics simulations have concluded that the catalytic domain of CDC25B may experience a significant degree of dynamics...
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04-18-2014 01:35 PM
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Protein Expr Purif. 2011 Aug 31;
Authors: Chen W, Gamache E, Richardson D, Du Z, Wang C
Abstract
Alzheimer's disease (AD) is the most common type of dementia in elderly people. Senile plaques, a pathologic hallmark of AD, are composed of amyloid ? peptide (A?). A? aggregation produces...
[NMR paper] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14
Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C
PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...
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11-24-2010 08:49 PM
[NMR paper] NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin
NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Jan 14;275(2):1089-94
Authors: Huang W, Dolmer K, Liao X, Gettins PG
Human alpha(2)-macroglobulin-proteinase complexes bind to their receptor, the low density lipoprotein receptor-related protein (LRP), through a discrete 138-residue C-terminal receptor binding domain (RBD), which also binds to the beta-amyloid peptide. We have used NMR...
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[NMR paper] Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bil
Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
Biochemistry. 1997 Oct 14;36(41):12616-24
Authors: Jones DH, Rigby AC, Barber KR, Grant CW
During the course of a previous study by wideline 2H NMR, we noted spectral features suggesting the possibility of monitoring homodimer/oligomer interactions between...
Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.
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