Binding mechanism of the matrix domain of HIV-1 gag on lipid membranes.
matrix domain of hiv-1
membrane modeling
membrane targeting proteins
molecular biophysics
molecular dynamics
none
protein-lipid interactions
structural biology
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
18 08 2020
18 08 2020
Historique:
received:
06
05
2020
accepted:
14
08
2020
pubmed:
19
8
2020
medline:
12
2
2021
entrez:
19
8
2020
Statut:
epublish
Résumé
Specific protein-lipid interactions are critical for viral assembly. We present a molecular dynamics simulation study on the binding mechanism of the membrane targeting domain of HIV-1 Gag protein. The matrix (MA) domain drives Gag onto the plasma membrane through electrostatic interactions at its highly-basic-region (HBR), located near the myristoylated (Myr) N-terminus of the protein. Our study suggests Myr insertion is involved in the sorting of membrane lipids around the protein-binding site to prepare it for viral assembly. Our realistic membrane models confirm interactions with PIP
Identifiants
pubmed: 32808928
doi: 10.7554/eLife.58621
pii: 58621
pmc: PMC7476761
doi:
pii:
Substances chimiques
Membrane Lipids
0
gag Gene Products, Human Immunodeficiency Virus
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM063796
Pays : United States
Organisme : National Science Foundation
ID : ACI-1548562
Pays : International
Organisme : NIGMS NIH HHS
ID : R01 GM116961
Pays : United States
Informations de copyright
© 2020, Monje-Galvan and Voth.
Déclaration de conflit d'intérêts
VM, GV No competing interests declared
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