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. 2015 Jun 15;7(6):3076–3115. doi: 10.3390/v7062761

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Cocksfoot mottle virus capsid. Sobemovirus capsid is assembled according to T=3 icosahedral lattice symmetry. The CP monomers are chemically identical but exist in three slightly different conformations, denoted as A (blue), B (red) and C (green) subunits. The A, B and C subunits build one icosahedral subunit (on the left). Altogether, there are 60 icosahedral subunits per sobemoviral T=3 particle (on the right). The A subunits interact at the icosahedral fivefold axes to form 12 pentamers while the pairs of B and C subunits meet at icosahedral threefold axes to form 20 hexamers. The pentamers and hexamers differ significantly in shape—hexamers are generally planar and pentamers are substantially bent. The combination of hexamers and pentamers gives the particle its characteristic shape. Pictures taken from http://viperdb.scripps.edu [146].