Early stages of the HIV-1 capsid protein lattice formation.
The early stages in the formation of the HIV-1 capsid (CA) protein lattice are investigated. The underlying coarse-grained (CG) model is parameterized directly from experimental data and examined under various native contact interaction strengths, CA dimer interfacial configurations, and local surface curvatures. The mechanism of early contiguous mature-style CA p6 lattice formation is explored, and a trimer-of-dimers structure is found to be crucial for CA lattice production. Quasi-equivalent generation of both the pentamer and hexamer components of the HIV-1 viral CA is also demonstrated, and the formation of pentamers is shown to be highly sensitive to local curvature, supporting the view that such inclusions in high-curvature regions allow closure of the viral CA surface. The complicated behavior of CA lattice self-assembly is shown to be reducible to a relatively simple function of the trimer-of-dimers behavior.
Department of Chemistry, University of Chicago, Chicago, Illinois, USA.
John M A
JM
Grime
Gregory A
GA
Voth
D002213:Capsid / Q000737:chemistry / Q000378:metabolism; D036022:Capsid Proteins / Q000737:chemistry*; D015497:HIV-1 / Q000737:chemistry / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D055503:Protein Multimerization; D054301:gag Gene Products, Human Immunodeficiency Virus / Q000737:chemistry
D036022:Capsid Proteins; D054301:gag Gene Products, Human Immunodeficiency Virus; C083002:p6 gag protein, Human immunodeficiency virus 1