$MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography$
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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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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5393cc79aa8d46d7b03a93a616d4e3b9
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spelling	oai:doaj.org-article:5393cc79aa8d46d7b03a93a616d4e3b92021-12-02T15:36:28ZMyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography10.1038/s41467-021-22590-62041-1723https://doaj.org/article/5393cc79aa8d46d7b03a93a616d4e3b92021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22590-6https://doaj.org/toc/2041-1723MAL 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.Max T. B. ClabbersSusannah HolmesTimothy W. MuusseParimala R. VajjhalaSara J. ThygesenAlpeshkumar K. MaldeDominic J. B. HunterTristan I. CrollLeonie FlueckigerJeffrey D. NansonMd. Habibur RahamanAndrew AquilaMark S. HunterMengning LiangChun Hong YoonJingjing ZhaoNadia A. ZatsepinBrian AbbeyEmma SiereckiYann GambinKatryn J. StaceyConnie DarmaninBostjan KobeHongyi XuThomas VeNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
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 Portfolio
publishDate	2021
url	https://doaj.org/article/5393cc79aa8d46d7b03a93a616d4e3b9
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MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography

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