Preparation of a stable CCL5·CCR5·G
Chemokine purification
Chemokine receptor purification
G protein coupled receptor (GPCR)
GPCR•G protein complex assembly
HIV
Insect cell expression
Membrane protein structure
Journal
Methods in cell biology
ISSN: 0091-679X
Titre abrégé: Methods Cell Biol
Pays: United States
ID NLM: 0373334
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
27
5
2022
pubmed:
28
5
2022
medline:
1
6
2022
Statut:
ppublish
Résumé
The numerous chemokines and their cognate G protein-coupled chemokine receptors on the surface of leukocytes form a complex signaling network, which regulates the immune response and also other key physiological processes. Currently only a very limited number of structures of chemokine•chemokine receptor complexes have been solved. More structures are needed for the understanding of their mechanism of action and the rational design of drugs against these highly relevant therapeutic targets. Recently, we have determined the cryo-EM structure of the human wild-type CCR5 chemokine receptor, which is also the HIV-1 coreceptor, in its active conformation bound to the chemokine super-agonist [6P4]CCL5 and the heterotrimeric G
Identifiants
pubmed: 35623699
pii: S0091-679X(22)00033-4
doi: 10.1016/bs.mcb.2022.03.001
pii:
doi:
Substances chimiques
CCL5 protein, human
0
CCR5 protein, human
0
Chemokine CCL5
0
Chemokines
0
Receptors, CCR5
0
Receptors, G-Protein-Coupled
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
115-141Informations de copyright
Copyright © 2022 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare no conflict of interest.