Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form.

Détails

ID Serval
serval:BIB_03ECE6599B4F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form.
Périodique
Biomolecular NMR Assignments
Auteur(s)
Ravotti F., Sborgi L., Cadalbert R., Huber M., Mazur A., Broz P., Hiller S., Meier B.H., Böckmann A.
ISSN
1874-270X (Electronic)
ISSN-L
1874-270X
Statut éditorial
Publié
Date de publication
2016
Peer-reviewed
Oui
Volume
10
Numéro
1
Pages
107-115
Langue
anglais
Résumé
The apoptosis-associated speck-like protein (ASC protein) plays a central role in eukaryotic innate immune response. Upon infection, multiple ASC molecules assemble into long filaments, which are fundamental for triggering the cellular defense mechanism by starting an inflammatory cascade with the activation of caspase-1. ASC is composed of two domains, the C-terminal caspase-recruitment domain, which is involved in the recruitment of the caspase, and the N-terminal PYRIN domain (PYD), which is responsible for the formation of the filament. Here we present the (13)C and (15)N chemical shift assignment for filaments formed by the PYD of mouse ASC, a 91-residue protein. The backbone between residues 4 and 84 is assigned without interruption. Also, 86 % of the sidechain resonances for this stretch are assigned. Residues 1-3 and 85-91 show unfavorable dynamics and are not observed. Secondary chemical-shift analysis shows the presence of six α-helices.

Mots-clé
Amino Acid Sequence, Animals, Apoptosis Regulatory Proteins/chemistry, CARD Signaling Adaptor Proteins, Mice, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Pyrin Domain, Filament, Mouse ASC PYRIN domain, Sequential assignments, Solid-state NMR
Pubmed
Web of science
Création de la notice
25/10/2017 11:05
Dernière modification de la notice
20/08/2019 13:25
Données d'usage