Structural basis for GTP-induced dimerization and antiviral function of guanylate-binding proteins.
GTP-induced dimerization
antiviral factors
furin inhibition
guanylate-binding proteins
innate immunity
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
13 04 2021
13 04 2021
Historique:
entrez:
20
4
2021
pubmed:
21
4
2021
medline:
27
11
2021
Statut:
ppublish
Résumé
Guanylate-binding proteins (GBPs) form a family of dynamin-related large GTPases which mediate important innate immune functions. They were proposed to form oligomers upon GTP binding/hydrolysis, but the molecular mechanisms remain elusive. Here, we present crystal structures of C-terminally truncated human GBP5 (hGBP5
Identifiants
pubmed: 33876762
pii: 2022269118
doi: 10.1073/pnas.2022269118
pmc: PMC8054025
pii:
doi:
Substances chimiques
GBP5 protein, human
0
env Gene Products, Human Immunodeficiency Virus
0
Guanosine Triphosphate
86-01-1
GBP2 protein, human
EC 3.6.1.-
GTP-Binding Proteins
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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