v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | The Gag protein from retroviruses, also known as p24, forms the inner protein layer of the nucleocapsid. It is composed of two domains, the N-terminal domain (NTD), which contributes to viral core formation, and the C-terminal domain (CTD), which is required for capsid dimerisation, Gag oligomerization and viral formation [, ]. This protein performs highly complex orchestrated tasks during the assembly, budding, maturation and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. ELISA tests for p24 is the most commonly used method to demonstrate virus replication both in vivoand in vitro[ , ].This is the C-terminal domain of retroviral p24 nucleocapsid protein, which contains a highly conserved region across retroviruses, the major homology region (MHR). The MHR is essential for the stability and folding of the monomer and hence for viral assembly, maturation and infectivity. This is a globular domain, composed of four helices and an extended N-terminal strand that forms a dimer through parallel packing of helix 2. The MHR dimer is a target for the development of anti-HIV drugs [, , ]. |
| Short Name | Gag_p24_C |