5DCK
Crystal Structure of FIV Capsid C-Terminal Domain
Summary for 5DCK
| Entry DOI | 10.2210/pdb5dck/pdb |
| Descriptor | Capsid C-Terminal Domain (2 entities in total) |
| Functional Keywords | retrovirus, fiv, capsid, viral protein |
| Biological source | Feline immunodeficiency virus (isolate Petaluma) (FIV) |
| Cellular location | Matrix protein p15: Virion . Capsid protein p24: Virion . Nucleocapsid protein p13: Virion : P16087 |
| Total number of polymer chains | 2 |
| Total formula weight | 16506.67 |
| Authors | Galilee, M.,Khwaja, A.,Alian, A. (deposition date: 2015-08-24, release date: 2016-04-20, Last modification date: 2024-01-10) |
| Primary citation | Khwaja, A.,Galilee, M.,Marx, A.,Alian, A. Structure of FIV capsid C-terminal domain demonstrates lentiviral evasion of genetic fragility by coevolved substitutions. Sci Rep, 6:24957-24957, 2016 Cited by PubMed Abstract: Viruses use a strategy of high mutational rates to adapt to environmental and therapeutic pressures, circumventing the deleterious effects of random single-point mutations by coevolved compensatory mutations, which restore protein fold, function or interactions damaged by initial ones. This mechanism has been identified as contributing to drug resistance in the HIV-1 Gag polyprotein and especially its capsid proteolytic product, which forms the viral capsid core and plays multifaceted roles in the viral life cycle. Here, we determined the X-ray crystal structure of C-terminal domain of the feline immunodeficiency virus (FIV) capsid and through interspecies analysis elucidate the structural basis of co-evolutionarily and spatially correlated substitutions in capsid sequences, which when otherwise uncoupled and individually substituted into HIV-1 capsid impair virion assembly and infectivity. The ability to circumvent the deleterious effects of single amino acid substitutions by cooperative secondary substitutions allows mutational flexibility that may afford viruses an important survival advantage. The potential of such interspecies structural analysis for preempting viral resistance by identifying such alternative but functionally equivalent patterns is discussed. PubMed: 27102180DOI: 10.1038/srep24957 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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