ATP-binding and hydrolysis of human NLRP3

Rebecca Brinkschulte; David M. Fußhöller; Florian Hoss; Juan F. Rodríguez-Alcázar; Mario A. Lauterbach; Carl-Christian Kolbe; Melanie Rauen; Semra Ince; Christian Herrmann; Eicke Latz; Matthias Geyer

doi:10.1038/s42003-022-04120-2

Communications Biology (Nov 2022)

ATP-binding and hydrolysis of human NLRP3

Rebecca Brinkschulte,
David M. Fußhöller,
Florian Hoss,
Juan F. Rodríguez-Alcázar,
Mario A. Lauterbach,
Carl-Christian Kolbe,
Melanie Rauen,
Semra Ince,
Christian Herrmann,
Eicke Latz,
Matthias Geyer

Affiliations

Rebecca Brinkschulte: Institute of Structural Biology, University of Bonn
David M. Fußhöller: Institute of Structural Biology, University of Bonn
Florian Hoss: Institute of Innate Immunity, University of Bonn
Juan F. Rodríguez-Alcázar: Institute of Innate Immunity, University of Bonn
Mario A. Lauterbach: Institute of Innate Immunity, University of Bonn
Carl-Christian Kolbe: Institute of Innate Immunity, University of Bonn
Melanie Rauen: Institute of Structural Biology, University of Bonn
Semra Ince: Physical Chemistry I, Ruhr University Bochum
Christian Herrmann: Physical Chemistry I, Ruhr University Bochum
Eicke Latz: Institute of Innate Immunity, University of Bonn
Matthias Geyer: Institute of Structural Biology, University of Bonn

DOI: https://doi.org/10.1038/s42003-022-04120-2
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 12

Abstract

Read online

Analysis of the inflammasome-forming protein NLRP3 provides insights into the function of conserved residues in the ATP-binding site of NLRP3 and the correlation of ATP hydrolysis with inflammasome activation.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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