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Updated: Apr 15, 2026

Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
Published on: August 9, 2011
Early stage P22 viral capsid self-assembly mediated by scaffolding protein: atom-resolved model and molecular
Jiajian Jiang1, Jing Yang1, Yuriy V Sereda1
1Center for Theoretical and Computational Nanoscience, Department of Chemistry, Indiana University, Bloomington, Indiana 47405, United States.
Abstract:
Molecular dynamics simulation of an atom-resolved bacteriophage P22 capsid model is used to delineate the underlying mechanism of early stage P22 self-assembly. A dimer formed by the C-terminal fragment of scaffolding protein with a new conformation is demonstrated to catalyze capsomer (hexamer and pentamer) aggregation efficiently. Effects of scaffolding protein/coat protein binding patterns and scaffolding protein concentration on efficiency, fidelity, and capsid curvature of P22 self-assembly are identified.
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