Function
The function of the HIV-1 capsid protein is to encapsidate and protect the viral RNA genome. It contains important sites on its surface that allow the virion to be attach to the host cell. The CA protein a key has an important role in early and late stages of the HIV virus replication cycle.
The HIV capsid is built from a single protein, known as capsid protein (CA). The protein folds to form two domains the N-terminal and C-terminal connected by a small flexible linker.
Disease
HIV infection (Human Immunodeficiency virus) The virus attacks the cells in the body that help to fight infection, causing weakness in the immune system and making the person’s liable for any infection or disease. HIV can be spread by unprotected intercourse, blood, breast milk, body fluids.
Relevance
The studies of the HIV capsid in this case Mutagenesis and structural experiments have revealed that capsid core stability affects uncoating and initiation of reverse transcription in host cells. The studies have led to efforts in developing antivirals targeting the capsid protein and its assembly.
Structural highlights
Mutant of the HIV-1 Capsid p.The structure on the scene is the E28A mutant of the HIV-1 Capsid protein. The green balls are the Cl ion and the purple are Iodide ions. The structure was loaded and the color was changed to model the 6 chains connected together by a flexible linker to form the hexamers which encloses the viral RNA.
Scene two structural highlights
Spacefill mutant HIV-1, the image displays the 6 proteins connected forming the hexamer and the N terminal domain pocket in the center this is important because is not a crucial binding site and displays low backbone deformation and mobility and shows less hydrogen binding which makes it a good target area to create an antiviral inhibitor.
Scene three structural highlights
Ca Hexamer interfaces, this is the image of the backbone of the inner surface of the CA, that is formed by two neighboring CA N- terminal domain interface pocked and is capped at one end by the R18 sidechains and by interaction of the E28-K30 on the other end. The two side chains are slightly separated that it is difficult to form hydrogen bonding. This led to explore the identification of sensitive interactions of the CA interfaces using biochemical analysis that lead to develop new antivirals targeting the stability of CA assemblies.
