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All-atom models of the membrane-spanning domain of HIV-1 gp41 from metadynamics
Journal article   Open access   Peer reviewed

All-atom models of the membrane-spanning domain of HIV-1 gp41 from metadynamics

Vamshi K Gangupomu and Cameron F Abrams
Biophysical journal, v 99(10), pp 3438-3444
17 Nov 2010
PMID: 21081093
url
https://doi.org/10.1016/j.bpj.2010.09.054View
Published, Version of Record (VoR) Open

Abstract

Protein Structure, Tertiary Thermodynamics HIV-1 - chemistry Water - chemistry Models, Molecular Lipid Bilayers - chemistry Protein Stability HIV Envelope Protein gp41 - chemistry Molecular Dynamics Simulation Arginine - chemistry
The 27-residue membrane-spanning domain (MSD) of the HIV-1 glycoprotein gp41 bears conserved sequence elements crucial to the biological function of the virus, in particular a conserved GXXXG motif and a midspan arginine. However, structure-based explanations for the roles of these and other MSD features remain unclear. Using molecular dynamics and metadynamics calculations of an all-atom, explicit solvent, and membrane-anchored model, we study the conformational variability of the HIV-1 gp41 MSD. We find that the MSD peptide assumes a stable tilted α-helical conformation in the membrane. However, when the side chain of the midspan Arg (694) "snorkels" to the outer leaflet of the viral membrane, the MSD assumes a metastable conformation where the highly-conserved N-terminal core (between Lys(681) and Arg(694) and containing the GXXXG motif) unfolds. In contrast, when the Arg(694) side chain snorkels to the inner leaflet, the MSD peptide assumes a metastable conformation consistent with experimental observations where the peptide kinks at Phe(697) to facilitate Arg(694) snorkeling. Both of these models suggest specific ways that gp41 may destabilize viral membrane, priming the virus for fusion with a target cell.

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Biophysics
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