[NMR paper] 1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD).
1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD).
1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD).
Biomol NMR Assign. 2018 Jun 05;:
Authors: Baudin A, Guichard A, Collie GW, Rousseau S, Chaignepain S, Hocquellet A, Berbon M, Loquet A, Mackereth C, Guichard G, Odaert B
Abstract
Death receptors (DR) selectively drive cancer cells to apoptosis upon binding to the Tumor necrosis factor-a-Related Apoptosis-Inducing Ligand (TRAIL). Complex formation induces the oligomerization of the death receptors DR4 (TRAIL-R1) and DR5 (TRAIL-R2) and transduces the apoptogenic signal to their respective death domains, leading to Death Inducing Signaling Complex (DISC) formation, caspase activation and ultimately cell death. Several crystal structures of the ExtraCellular Domain from Death Receptor 5 (DR5-ECD) have been reported in complex with the TRAIL ligand or anti-DR5 antibodies, but none for the isolated protein. In order to fill this gap and to perform binding experiments with TRAIL peptidomimetics, we have produced isotopically labelled DR5-ECD and started a conformational analysis by using high-field 3D NMR spectroscopy. Herein, we present the first resonance assignment of a TRAIL receptor in solution and the determination of its secondary structure from NMR chemical shifts.
PMID: 29869749 [PubMed - as supplied by publisher]
[NMR paper] NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand.
NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand.
Related Articles NMR resonance assignments of the FKBP domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) in complex with a farnesyl ligand.
Biomol NMR Assign. 2017 Feb 24;:
Authors: Yu L, Yadav RP, Artemyev NO
Abstract
Aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) is a specialized chaperone of phosphodiesterase 6, a key effector enzyme in...
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[NMR paper] NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
Biomol NMR Assign. 2016 Jun 29;
Authors: Amin N, Nietlispach D, Qamar S, Coyle J, Chiarparin E, Williams G
Abstract
Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic...
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07-01-2016 03:22 PM
[NMR paper] (15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
(15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles (15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody.
Biomol NMR Assign. 2013 Jan 29;
Authors: Prosser CE, Waters LC, Muskett FW, Veverka V, Addis PW, Griffin LM, Baker TS,...
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02-03-2013 10:19 AM
[NMR paper] NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
Biomol NMR Assign. 2013 Jan 17;
Authors: Vajpai N, Schott AK, Vogtherr M, Breeze AL
Abstract
Members of the fibroblast growth factor receptor tyrosine kinase family (FGFR1-4) play an important role in many...
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[NMR paper] Sequence-specific 1H NMR resonance assignments and secondary structure of human apoli
Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Related Articles Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Biochem Cell Biol. 1998;76(2-3):267-75
Authors: Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we...
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11-17-2010 11:06 PM
[NMR paper] Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human
Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
Protein Sci. 1997 Feb;6(2):383-90
...
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08-22-2010 03:31 PM
[NMR paper] Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human
Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
Protein Sci. 1997 Feb;6(2):383-90
...
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[NMR paper] Proton NMR sequence-specific assignments and secondary structure of a receptor bindin
Proton NMR sequence-specific assignments and secondary structure of a receptor binding domain of mouse gamma-interferon.
Related Articles Proton NMR sequence-specific assignments and secondary structure of a receptor binding domain of mouse gamma-interferon.
Biochemistry. 1993 Jun 1;32(21):5650-5
Authors: Sakai TT, Jablonsky MJ, DeMuth PA, Krishna NR, Jarpe MA, Johnson HM
Previous studies using synthetic peptides and monoclonal antibodies have implicated the N-terminal 39-residue segment as a receptor binding region of mouse gamma-interferon...
1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD).
Linear Mode
