Specific inter-domain interactions stabilize a compact HIV-1 Gag conformation.
HIV-1 Gag is a large multidomain poly-protein with flexible unstructured linkers connecting its globular subdomains. It is compact when in solution but assumes an extended conformation when assembled within the immature HIV-1 virion. Here, we use molecular dynamics (MD) simulations to quantitatively...
Main Authors: | , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2019-01-01
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Series: | PLoS ONE |
Online Access: | https://doi.org/10.1371/journal.pone.0221256 |