Related ArticlesToll-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 adaptive immune systems. The role of the transmembrane domain in TLR signaling is still elusive, while its importance for the TLR activation was clearly demonstrated. In the present study the ability of the TLR3 transmembrane domain to form dimers and trimers in detergent micelles was shown by solution NMR spectroscopy. Spatial structures and free energy magnitudes were determined for the TLR3 transmembrane domain in dimeric and trimeric states, and two possible surfaces that may be used for the helix-helix interaction by the full-length TLR3 were revealed.
[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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[NMR paper] Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
Chem Phys Lipids. 2013 Sep 24;
Authors: Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C
Abstract
The chloroplast twin arginine translocation...
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10-01-2013 11:15 PM
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Publication date: Available online 24 September 2013
Source:Chemistry and Physics of Lipids</br>
Author(s): Lei Zhang , Lishan Liu , Sergey Maltsev , Gary A. Lorigan , Carole Dabney-Smith</br>
The chloroplast twin arginine translocation system transports highly folded precursor proteins across the thylakoid using the protonmotive force as its only energy source. Hcf106 and another thylakoid protein, cpTatC compose the precursor receptor...
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09-25-2013 11:15 AM
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells.
Chembiochem. 2011 Mar 21;12(5):695-9
Authors: Potenza D, Vasile F, Belvisi L, Civera M, Araldi EM
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07-19-2011 07:52 PM
[NMR paper] 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of
15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores.
Related Articles 15N and 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores.
J Magn Reson. 2005 Apr;173(2):322-7
Authors: Chekmenev EY, Hu J, Gor'kov PL, Brey WW, Cross TA, Ruuge A, Smirnov AI
This communication reports the first...
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11-25-2010 08:21 PM
Solution NMR Investigation of the CD95/FADD Homotypic Death Domain Complex Suggests L
Solution NMR Investigation of the CD95/FADD Homotypic Death Domain Complex Suggests Lack of Engagement of the CD95 C Terminus.
Related Articles Solution NMR Investigation of the CD95/FADD Homotypic Death Domain Complex Suggests Lack of Engagement of the CD95 C Terminus.
Structure. 2010 Oct 13;18(10):1378-90
Authors: Esposito D, Sankar A, Morgner N, Robinson CV, Rittinger K, Driscoll PC
We have addressed complex formation between the death domain (DD) of the death receptor CD95 (Fas/APO-1) with the DD of immediate adaptor protein FADD using nuclear...
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10-16-2010 03:56 PM
[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...
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08-22-2010 05:08 PM
[NMR paper] Structural characterization of peptide hormone/receptor interactions by NMR spectrosc
Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy.
Biopolymers. 1999;51(3):208-20
Authors: Pellegrini M, Mierke DF
The structural characterization of peptide hormones and their interaction with G-protein (guanine nucleotide-binding regulatory protein) coupled...
Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
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