MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
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 microcry...
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Nature Publishing Group
2021-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-22590-6 |
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doaj-5393cc79aa8d46d7b03a93a616d4e3b92021-05-11T14:48:36ZengNature Publishing GroupNature Communications2041-17232021-05-0112111410.1038/s41467-021-22590-6MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallographyMax T. B. Clabbers0Susannah Holmes1Timothy W. Muusse2Parimala R. Vajjhala3Sara J. Thygesen4Alpeshkumar K. Malde5Dominic J. B. Hunter6Tristan I. Croll7Leonie Flueckiger8Jeffrey D. Nanson9Md. Habibur Rahaman10Andrew Aquila11Mark S. Hunter12Mengning Liang13Chun Hong Yoon14Jingjing Zhao15Nadia A. Zatsepin16Brian Abbey17Emma Sierecki18Yann Gambin19Katryn J. Stacey20Connie Darmanin21Bostjan Kobe22Hongyi Xu23Thomas Ve24Department of Materials and Environmental Chemistry, Stockholm UniversityAustralian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe UniversitySchool of Chemistry and Molecular Biosciences, The University of QueenslandSchool of Chemistry and Molecular Biosciences, The University of QueenslandSchool of Chemistry and Molecular Biosciences, The University of QueenslandInstitute for Glycomics, Griffith UniversitySchool of Chemistry and Molecular Biosciences, The University of QueenslandCambridge Institute for Medical Research, University of CambridgeAustralian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe UniversitySchool of Chemistry and Molecular Biosciences, The University of QueenslandSchool of Chemistry and Molecular Biosciences, The University of QueenslandLinac Coherent Light Source, SLAC National Accelerator LaboratoryLinac Coherent Light Source, SLAC National Accelerator LaboratoryLinac Coherent Light Source, SLAC National Accelerator LaboratoryLinac Coherent Light Source, SLAC National Accelerator LaboratoryDepartment of Materials and Environmental Chemistry, Stockholm UniversityAustralian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe UniversityAustralian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe UniversityEMBL Australia Node in Single Molecule Science, University of New South WalesEMBL Australia Node in Single Molecule Science, University of New South WalesSchool of Chemistry and Molecular Biosciences, The University of QueenslandAustralian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe UniversitySchool of Chemistry and Molecular Biosciences, The University of QueenslandDepartment of Materials and Environmental Chemistry, Stockholm UniversityInstitute for Glycomics, Griffith UniversityMAL 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.https://doi.org/10.1038/s41467-021-22590-6 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
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 |
| spellingShingle |
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 MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography Nature Communications |
| author_facet |
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 |
| author_sort |
Max T. B. Clabbers |
| title |
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography |
| title_short |
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography |
| title_full |
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography |
| title_fullStr |
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography |
| title_full_unstemmed |
MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography |
| title_sort |
myd88 tir domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2021-05-01 |
| description |
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. |
| url |
https://doi.org/10.1038/s41467-021-22590-6 |
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