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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Autor*in:	Max T. B. Clabbers [verfasserIn] Susannah Holmes [verfasserIn] Timothy W. Muusse [verfasserIn] Parimala R. Vajjhala [verfasserIn] Sara J. Thygesen [verfasserIn] Alpeshkumar K. Malde [verfasserIn] Dominic J. B. Hunter [verfasserIn] Tristan I. Croll [verfasserIn] Leonie Flueckiger [verfasserIn] Jeffrey D. Nanson [verfasserIn] Md. Habibur Rahaman [verfasserIn] Andrew Aquila [verfasserIn] Mark S. Hunter [verfasserIn] Mengning Liang [verfasserIn] Chun Hong Yoon [verfasserIn] Jingjing Zhao [verfasserIn] Nadia A. Zatsepin [verfasserIn] Brian Abbey [verfasserIn] Emma Sierecki [verfasserIn] Yann Gambin [verfasserIn] Katryn J. Stacey [verfasserIn] Connie Darmanin [verfasserIn] Bostjan Kobe [verfasserIn] Hongyi Xu [verfasserIn] Thomas Ve [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Übergeordnetes Werk:	In: Nature Communications - Nature Portfolio, 2016, 12(2021), 1, Seite 14
Übergeordnetes Werk:	volume:12 ; year:2021 ; number:1 ; pages:14

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1038/s41467-021-22590-6

Katalog-ID:	DOAJ008653364

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author	Max T. B. Clabbers
spellingShingle	Max T. B. Clabbers misc Science misc Q MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
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topic_title	MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
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title	MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
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author_browse	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
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title_sort	myd88 tir domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
title_auth	MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
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.
abstractGer	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.
abstract_unstemmed	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.
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title_short	MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography
url	https://doi.org/10.1038/s41467-021-22590-6 https://doaj.org/article/5393cc79aa8d46d7b03a93a616d4e3b9 https://doaj.org/toc/2041-1723
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MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography

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