Structural characterization of TIR-domain signalosomes through a combination of structural biology approaches.
IUCrJ
; 11(Pt 5): 695-707, 2024 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-39190506
ABSTRACT
The TIR (Toll/interleukin-1 receptor) domain represents a vital structural element shared by proteins with roles in immunity signalling pathways across phyla (from humans and plants to bacteria). Decades of research have finally led to identifying the key features of the molecular basis of signalling by these domains, including the formation of open-ended (filamentous) assemblies (responsible for the signalling by cooperative assembly formation mechanism, SCAF) and enzymatic activities involving the cleavage of nucleotides. We present a historical perspective of the research that led to this understanding, highlighting the roles that different structural methods played in this process X-ray crystallography (including serial crystallography), microED (micro-crystal electron diffraction), NMR (nuclear magnetic resonance) spectroscopy and cryo-EM (cryogenic electron microscopy) involving helical reconstruction and single-particle analysis. This perspective emphasizes the complementarity of different structural approaches.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transdução de Sinais
/
Microscopia Crioeletrônica
Limite:
Humans
Idioma:
En
Revista:
IUCrJ
Ano de publicação:
2024
Tipo de documento:
Article