Molecular Structure of human NLRP3 solved

February 03, 2022

Apical view on the NLRP3 decamer (picture: Nature / Hochheiser et.al.)

 

Elucidating the structure of a central inflammatory switch provides the basis for the development of powerful anti-inflammatory therapeutic tools

ImmunoSensation2 Member Prof. Matthias Geyer and his team, in collaboration with researchers at the University of Regensburg, have solved the structure of a central cellular inflammatory switch: NLRP3. Cryo Electron Microscopy (Cryo-EM) analysis revealed NLRP3 to form a decameric structure when incubated with the inhibitor CRID3 (Cytokine Release Inhibitory Drug 3). Identifying the CRID3 binding-site as well as solving the overall structure of human NLRP3 now provides the basis to further elucidate the molecular mechanisms leading to activation of NLRP3, as well es the development of potent anti-inflammatory pharmaceuticals. The results are published in the journal Nature.

Publication:

Inga V. Hochheiser et. al. (2022), Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3; Nature; DOI: 10.1038/s41586-022-04467-w

Contact:

Prof. Dr. Matthias Geyer Institute of Structural Biology at the University of Bonn Phone: +49-228/287-51400 E-mail: matthias.geyer@uni-bonn.de