MyD88 TIR domain higher-order assembly interactions revealed by microcrystal electron diffraction and serial femtosecond crystallography.
Crystallography
/ methods
Dimerization
HEK293 Cells
Humans
Membrane Glycoproteins
/ chemistry
Models, Molecular
Molecular Dynamics Simulation
Mutation
Myeloid Differentiation Factor 88
/ chemistry
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Domains
Receptors, Interleukin-1
/ chemistry
Recombinant Proteins
Signal Transduction
/ genetics
Toll-Like Receptor 4
/ chemistry
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
10 05 2021
10 05 2021
Historique:
received:
24
12
2020
accepted:
18
03
2021
entrez:
11
5
2021
pubmed:
12
5
2021
medline:
3
6
2021
Statut:
epublish
Résumé
MyD88 and MAL are Toll-like receptor (TLR) adaptors that signal to induce pro-inflammatory cytokine production. We previously observed that the TIR domain of MAL (MAL
Identifiants
pubmed: 33972532
doi: 10.1038/s41467-021-22590-6
pii: 10.1038/s41467-021-22590-6
pmc: PMC8110528
doi:
Substances chimiques
MYD88 protein, human
0
Membrane Glycoproteins
0
Myeloid Differentiation Factor 88
0
Receptors, Interleukin-1
0
Recombinant Proteins
0
TIRAP protein, human
0
TLR4 protein, human
0
Toll-Like Receptor 4
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
2578Subventions
Organisme : Wellcome Trust
ID : 209407/Z/17/Z
Pays : United Kingdom
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