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The genome and proteins of HIV (human immunodeficiency virus) have been the subject of extensive research since the discovery of the virus in 1983. [1] [2] "In the search for the causative agent, it was initially believed that the virus was a form of the Human T-cell leukemia virus (HTLV), which was known at the time to affect the human immune system and cause certain leukemias.
The HIV capsid consists of roughly 2000 copies of the p24 protein. The p24 structure is shown in two representations: cartoon (top) and isosurface (bottom) The p24 capsid protein is the most abundant HIV protein with each virus containing approximately 1,500 to 3,000 p24 molecules. [1]
HIV-1 protease labelled according to its resemblance to an English Bulldog or a fat cat. [7] The blue and cyan-green ribbons depict the peptide backbone of a wild-type ( ) and a mutant ( ) structure, respectively. Mature HIV protease exists as a 22 kDa homodimer, with each subunit made up of 99 amino acids. [1]
The viral envelope contains proteins from the host cell and relatively few copies of the HIV envelope protein, [24] which consists of a cap made of three molecules known as glycoprotein (gp) 120, and a stem consisting of three gp41 molecules that anchor the structure into the viral envelope.
Like other lentiviruses, HIV-1 encodes a trans-activating regulatory protein (Tat), which is essential for efficient transcription of the viral genome. [7] [8] Tat acts by binding to an RNA stem-loop structure, the trans-activation response element (TAR), found at the 5′ ends of nascent HIV-1 transcripts.
Structural depiction of the HIV catalytic core domain based on the works of Feng, L. and Kvaratskhelia, M. from the protein database. HIV integrase is a 32kDa viral protein consisting of three domains- N-terminus, catalytic core domain, and C-terminus, which each have distinct properties and functions contributing to the efficacy of HIV ...