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. 2023 Nov 30;15(11):mjad076. doi: 10.1093/jmcb/mjad076

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© The Author(s) (2023). Published by Oxford University Press on behalf of Journal of Molecular Cell Biology, CEMCS, CAS.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Assembly of the HIV-1 capsid. (A) Each capsid monomer is shown in cartoon representation, with CA-NTDs in light or dark cyan and CA-CTDs in wheat or olive. Light and dark shades represent monomers that contribute to capsid hexamers and pentamers, respectively. For illustration, on one monomer, α-helices are labelled sequentially, and the positions of N-terminal β-hairpin and Cyp-loop are indicated. (B) Capsid monomers pack into either hexamers (top) or pentamers (bottom). (C) The HIV-1 capsid (PDB: 3J3Q). Approximately 200–250 capsid hexamers combine with 12 capsid pentamers to form a closed fullerene cone structure. Hexamers are shown in cartoon representation. The 12 pentamers are distributed toward the ends of the structure and shown in surface representation.