Related ArticlesNMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
Structure. 2017 Mar 07;25(3):446-457
Authors: Chadwick AC, Jensen DR, Hanson PJ, Lange PT, Proudfoot SC, Peterson FC, Volkman BF, Sahoo D
Abstract
The interaction of high-density lipoprotein (HDL) with its receptor, scavenger receptor BI (SR-BI), is critical for lowering plasma cholesterol levels and reducing the risk for cardiovascular disease. The HDL/SR-BI complex facilitates delivery of cholesterol into cells and is likely mediated by receptor dimerization. This work describes the use of nuclear magnetic resonance (NMR) spectroscopy to generate the first high-resolution structure of the C-terminal transmembrane domain of SR-BI. This region of SR-BI harbors a leucine zipper dimerization motif, which when mutated impairs the ability of the receptor to bind HDL and mediate cholesterol delivery. These losses in function correlate with the inability of SR-BI to form dimers. We also identify juxtamembrane regions of the extracellular domain of SR-BI that may interact with the lipid surface to facilitate cholesterol transport functions of the receptor.
[NMR paper] NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
Related Articles NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
J Biol Chem. 2017 Mar 09;:
Authors: Sharma AK, Birrane GG, Anklin C, Rigby AC, Alper SL
Abstract
Nitrovasodilators relax vascular smooth muscle cells (VSMC) in part by modulating the interaction of the C-terminal...
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[NMR paper] Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.
Solution NMR studies reveal the location of the second transmembrane domain of the human sigma-1 receptor.
Related Articles Solution 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...
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[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...
[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] High resolution NMR solution structure of the leucine zipper domain of the c-Jun homo
High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
J Biol Chem. 1996 Jun 7;271(23):13663-7
Authors: Junius FK, O'Donoghue SI, Nilges M, Weiss AS, King GF
The solution structure of the c-Jun leucine zipper domain has been determined to high resolution using a new...
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[NMR paper] Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Biochemistry. 1996 Apr 16;35(15):4867-77
Authors: MacKay JP, Shaw GL, King GF
The backbone dynamics of the coiled-coil leucine zipper domain of c-Jun have been studied using proton-detected two-dimensional 1H-15N NMR spectroscopy. Longitudinal (T1) and transverse (T2) 15N relaxation times,...