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

Ravotti, Francesco and Sborgi, Lorenzo and Cadalbert, Riccardo and Huber, Matthias and Mazur, Adam and Broz, Petr and Hiller, Sebastian and Meier, Beat H. and Böckmann, Anja. (2016) Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form. Biomolecular NMR Assignments, 10 (1). pp. 107-115.

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Official URL: http://edoc.unibas.ch/44882/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Infection Biology (Broz)
05 Faculty of Science > Departement Biozentrum > Services Biozentrum > Research IT (Podvinec)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Broz, Petr and Hiller Odermatt, Sebastian and Mazur, Adam and Sborgi, Lorenzo and Podvinec, Michael
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:19 Dec 2017 13:29
Deposited On:18 Nov 2016 09:29

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