Nature Communications (May 2021)
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
- Max T. B. Clabbers,
- Susannah Holmes,
- Timothy W. Muusse,
- Parimala R. Vajjhala,
- Sara J. Thygesen,
- Alpeshkumar K. Malde,
- Dominic J. B. Hunter,
- Tristan I. Croll,
- Leonie Flueckiger,
- Jeffrey D. Nanson,
- Md. Habibur Rahaman,
- Andrew Aquila,
- Mark S. Hunter,
- Mengning Liang,
- Chun Hong Yoon,
- Jingjing Zhao,
- Nadia A. Zatsepin,
- Brian Abbey,
- Emma Sierecki,
- Yann Gambin,
- Katryn J. Stacey,
- Connie Darmanin,
- Bostjan Kobe,
- Hongyi Xu,
- Thomas Ve
Affiliations
- Max T. B. Clabbers
- Department of Materials and Environmental Chemistry, Stockholm University
- Susannah Holmes
- Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University
- Timothy W. Muusse
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Parimala R. Vajjhala
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Sara J. Thygesen
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Alpeshkumar K. Malde
- Institute for Glycomics, Griffith University
- Dominic J. B. Hunter
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Tristan I. Croll
- Cambridge Institute for Medical Research, University of Cambridge
- Leonie Flueckiger
- Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University
- Jeffrey D. Nanson
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Md. Habibur Rahaman
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Andrew Aquila
- Linac Coherent Light Source, SLAC National Accelerator Laboratory
- Mark S. Hunter
- Linac Coherent Light Source, SLAC National Accelerator Laboratory
- Mengning Liang
- Linac Coherent Light Source, SLAC National Accelerator Laboratory
- Chun Hong Yoon
- Linac Coherent Light Source, SLAC National Accelerator Laboratory
- Jingjing Zhao
- Department of Materials and Environmental Chemistry, Stockholm University
- Nadia A. Zatsepin
- Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University
- Brian Abbey
- Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University
- Emma Sierecki
- EMBL Australia Node in Single Molecule Science, University of New South Wales
- Yann Gambin
- EMBL Australia Node in Single Molecule Science, University of New South Wales
- Katryn J. Stacey
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Connie Darmanin
- Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University
- Bostjan Kobe
- School of Chemistry and Molecular Biosciences, The University of Queensland
- Hongyi Xu
- Department of Materials and Environmental Chemistry, Stockholm University
- Thomas Ve
- Institute for Glycomics, Griffith University
- DOI
- https://doi.org/10.1038/s41467-021-22590-6
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 14
Abstract
MAL and MyD88 are downstream adaptors of Toll-like receptors (TLR) and the MAL TIR domain forms filaments in vitro, which in turn nucleate the assembly of crystalline arrays of the MyD88 TIR domain. Here, the authors present the structure of these MyD88 TIR crystalline arrays solved by both microcrystal electron diffraction and serial femtosecond crystallography, and they show with mutagenesis experiments that MyD88 interface residues are important for TLR4 signaling in vivo.