Related ArticlesStructural Insights into ?-arrestin/CB1 Receptor Interaction: NMR and CD Studies on Model Peptides.
Int J Mol Sci. 2020 Oct 30;21(21):
Authors: Morales P, Bruix M, Jiménez MA
Abstract
Activation of the cannabinoid CB1 receptor induces different cellular signaling cascades through coupling to different effector proteins (G-proteins and ?-arrestins), triggering numerous therapeutic effects. Conformational changes and rearrangements at the intracellular domain of this GPCR receptor that accompany ligand binding dictate the signaling pathways. The GPCR-binding interface for G proteins has been extensively studied, whereas ?-arrestin/GPCR complexes are still poorly understood. To gain knowledge in this direction, we designed peptides that mimic the motifs involved in the putative interacting region: ?-arrestin1 finger loop and the transmembrane helix 7-helix 8 (TMH7-H8) elbow located at the intracellular side of the CB1 receptor. According to circular dichroism and NMR data, these peptides form a native-like, helical conformation and interact with each other in aqueous solution, in the presence of trifluoroethanol, and using zwitterionic detergent micelles as membrane mimics. These results increase our understanding of the binding mode of ?-arrestin and CB1 receptor and validate minimalist approaches to structurally comprehend complex protein systems.
[NMR paper] DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe.
DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe.
Related Articles DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe.
Nat Commun. 2020 Sep 25;11(1):4857
Authors: Liu Q, He QT, Lyu X, Yang F, Zhu ZL, Xiao P, Yang Z, Zhang F, Yang ZY, Wang XY, Sun P, Wang QW, Qu CX, Gong Z, Lin JY, Xu Z, Song SL, Huang SM, Guo SC, Han MJ, Zhu KK, Chen X, Kahsai AW, Xiao KH, Kong W, Li FH, Ruan...
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[NMR paper] Structural insights into the interaction of a monoclonal antibody and Nodal peptides by STD-NMR spectroscopy.
Structural insights into the interaction of a monoclonal antibody and Nodal peptides by STD-NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural insights into the interaction of a monoclonal antibody and Nodal peptides by STD-NMR spectroscopy.
Bioorg Med Chem. 2017 Dec 15;25(24):6589-6596
Authors: Calvanese L, Focà A, Sandomenico A, Focà G, Caporale A, Doti N, Iaccarino E, Leonardi A, D'Auria G, Ruvo M, Falcigno L
Abstract
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[NMR paper] Structural insight into the XTACC3/XMAP215 interaction from CD and NMR studies on model peptides.
Structural insight into the XTACC3/XMAP215 interaction from CD and NMR studies on model peptides.
Related Articles Structural insight into the XTACC3/XMAP215 interaction from CD and NMR studies on model peptides.
Biopolymers. 2017 Sep 18;:
Authors: Partida-Hanon A, Treviño MA, Mompeán M, Jiménez MÁ, Bruix M
Abstract
TACC3 is a centrosomal adaptor protein that plays important roles during mitotic spindle assembly. It interacts with chTOG/XMAP215, which catalyzes the addition of tubulin dimers during microtubule growth. A 3D...
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[NMR paper] Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study.
Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study.
Biophys J. 2016 Dec 20;111(12):2676-2688
Authors: Santos TL, Moraes A, Nakaie CR, Almeida FC, Schreier S, Valente AP
Abstract
A large number of antimicrobial peptides (AMPs) acts with high selectivity...
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[NMR paper] Investigation of the mechanism of action of novel amphipathic peptides: Insights from solid-state NMR studies of oriented lipid bilayers.
Investigation of the mechanism of action of novel amphipathic peptides: Insights from solid-state NMR studies of oriented lipid bilayers.
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Biochim Biophys Acta. 2014 Feb 6;
Authors: Fillion M, Noël M, Lorin A, Voyer N, Auger M
Abstract
We have investigated in the present study the effect of both non-selective and selective cationic 14-mer peptides on the lipid orientation of DMPC bilayers...
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02-11-2014 09:58 PM
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
High resolution NMR conformational studies of new bivalent NOP receptor antagonists in model membrane systems.
Bioorg Chem. 2011 Feb;39(1):59-66
Authors: Borioni A, Bastanzio G, Delfini M, Mustazza C, Sciubba F, Tatti M, Del Giudice MR
The interaction of new bivalent NOP receptor antagonists with dodecyl phosphatidylcholine micelles and DMPC/cholesterol liposomes was investigated in solution by high resolution NMR. The ligands are...
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[NMR paper] NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.
NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.
Related Articles NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.
J Mol Biol. 2004 Jun 18;339(5):1169-77
Authors: Bernini A, Ciutti A, Spiga O, Scarselli M, Klein S, Vannetti S, Bracci L, Lozzi L, Lelli B, Falciani C, Neri P, Niccolai N
The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several...
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[NMR paper] NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion prot
NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity.
Related Articles NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity.
J Biochem. 2000 Aug;128(2):271-81
Authors: Yoshida H, Matsushima N, Kumaki Y, Nakata M, Hikichi K
The N-terminal region of the prion protein from human and mouse contains five tandem repeats with the consensus...
Structural Insights into ?-arrestin/CB1 Receptor Interaction: NMR and CD Studies on Model Peptides.
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