The Notch signaling pathway, an important cell fate determination pathway, is modulated by the ubiquitin ligase Deltex. Here, we investigate the structural basis for Deltex-Notch interaction. We used nuclear magnetic resonance (NMR) spectroscopy to assign the backbone of the Drosophila Deltex WWE(2) domain and mapped the binding site of the Notch ankyrin (ANK) domain to the N-terminal WWE(A) motif. Using cultured Drosophila S2R+ cells, we find that point substitutions within the ANK-binding...
[ASAP] Identifying Distinct Structural Features of the SARS-CoV-2 Spike Protein Fusion Domain Essential for Membrane Interaction
Identifying Distinct Structural Features of the SARS-CoV-2 Spike Protein Fusion Domain Essential for Membrane Interaction
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00543/20210927/images/medium/bi1c00543_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00543
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09-29-2021 12:23 PM
Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling - Science
Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling - Science
Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling ScienceForkhead-associated (FHA) domains participate in phosphorylation-dependent signaling pathways by binding to phosphothreonine. As part of a signaling ...
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05-09-2019 11:40 PM
Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling - Science
Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling - Science
Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling ScienceForkhead-associated (FHA) domains participate in phosphorylation-dependent signaling pathways by binding to phosphothreonine. As part of a signaling ...
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05-09-2019 05:55 AM
[NMR paper] Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.
Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.
Protein Cell. 2017 01;8(1):67-71
Authors: Liu...
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01-10-2018 12:35 AM
[NMR paper] Segmental, domain-selective perdeuteration and small angle neutron scattering for structural analysis of multi-domain proteins
Segmental, domain-selective perdeuteration and small angle neutron scattering for structural analysis of multi-domain proteins
Multi-domain proteins play critical roles in fine-tuning essential processes in cellular signaling and gene regulation. Typically, multiple globular domains that are connected by flexible linkers undergo dynamic re-arrangements upon binding to protein, DNA or RNA ligands. RNA binding proteins (RBPs) represent an important class of multi-domain proteins, which regulate gene expression by recognizing linear or structured RNA sequence motifs. Here, we employ...
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06-21-2017 12:36 PM
[NMR paper] Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Biochemistry. 2014 May 20;53(19):3106-17
Authors: Gutte PG, Jurt S, Grütter MG, Zerbe O
Abstract
The cytosolic nucleotide-binding domain and leucine-rich repeat-containing receptors (NLRs)...
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07-06-2014 08:28 PM
Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
Unusual Structural Features Revealed by the SolutionNMR Structure of the NLRC5 Caspase Recruitment Domain
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi500177x/aop/images/medium/bi-2014-00177x_0007.gif
Biochemistry
DOI: 10.1021/bi500177x
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/0XcYOsOxzfs
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05-09-2014 07:01 PM
[NMR paper] Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and
Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and identification of the region that interacts with Ras.
Related Articles Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and identification of the region that interacts with Ras.
Drug Des Discov. 1996 Apr;13(3-4):83-93
Authors: Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC
The structure of the Ras-binding domain of human c-Raf-1 (residues 55 to 132) as determined in solution by NMR...