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EC Number	General Information	Commentary	Reference
3.4.23.B10	more	the C-terminal domain of RSV conserved capsid (CA) is arranged similarly to HIV-1 and M-PMV, whereas the N-terminal domain of CA adopts a novel arrangement in which the upstream p10 domain folds back into the CA lattice. In this position the cleavage site between CA and p10 appears to be inaccessible to the protease. Below CA, an extended density is consistent with the presence of a six-helix bundle formed by the spacer-peptide region. The cleavage between p10 and CA is indeed inhibited in the assembled lattice, a finding consistent with structural regulation of proteolytic maturation. Docking study and molecular dynamics flexible fitting. The major interaction across the dimeric interface occurs between adjacent hexamers at the CA-CTD is in the region of hydrophobic residues Pro426 and Val427 in helix 9. RSV has a cysteine residue (Cys431) at the base of helix 9 that has been speculated to participate in the interaction across the CA-CTD dimer interface. Modelling shows that the distance between Cys431 residues across the dimer interface is too large to permit disulfide bridge formation in the immature particle	754541
3.4.23.B10	physiological function	proteolytic cleavage of Gag by the viral protease (PR) is required for maturation of retroviruses from an immature form into an infectious form. Gag is cleaved by the viral protease enzyme into separate domains, leading to rearrangement of the virus into its infectious form	754541

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Release 2023.1 (January 2023)