HIV-1 Envelope Conformation, Allostery, and Dynamics.
HIV-1
allostery
envelope
molecular dynamics
structure
Journal
Viruses
ISSN: 1999-4915
Titre abrégé: Viruses
Pays: Switzerland
ID NLM: 101509722
Informations de publication
Date de publication:
07 05 2021
07 05 2021
Historique:
received:
07
04
2021
revised:
28
04
2021
accepted:
04
05
2021
entrez:
2
6
2021
pubmed:
3
6
2021
medline:
17
12
2021
Statut:
epublish
Résumé
The HIV-1 envelope glycoprotein (Env) mediates host cell fusion and is the primary target for HIV-1 vaccine design. The Env undergoes a series of functionally important conformational rearrangements upon engagement of its host cell receptor, CD4. As the sole target for broadly neutralizing antibodies, our understanding of these transitions plays a critical role in vaccine immunogen design. Here, we review available experimental data interrogating the HIV-1 Env conformation and detail computational efforts aimed at delineating the series of conformational changes connecting these rearrangements. These studies have provided a structural mapping of prefusion closed, open, and transition intermediate structures, the allosteric elements controlling rearrangements, and state-to-state transition dynamics. The combination of these investigations and innovations in molecular modeling set the stage for advanced studies examining rearrangements at greater spatial and temporal resolution.
Identifiants
pubmed: 34067073
pii: v13050852
doi: 10.3390/v13050852
pmc: PMC8150877
pii:
doi:
Substances chimiques
Antibodies, Neutralizing
0
HIV Antibodies
0
HIV Envelope Protein gp41
0
env Gene Products, Human Immunodeficiency Virus
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIAID NIH HHS
ID : R01 AI145687
Pays : United States
Organisme : NIAID NIH HHS
ID : P30 AI064518
Pays : United States
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