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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]
A diagram of the HIV spike protein (green), with the fusion peptide epitope highlighted in red, and a broadly neutralizing antibody (yellow) binding to the fusion peptide. As the sole viral protein on the surface of the virus, the envelope protein is a major target for HIV vaccine efforts. [28]
The primary env product is the protein gp160, which gets cleaved to gp120 (~480 amino acids) and gp41 (~345 amino acids) in the endoplasmatic reticulum by the cellular protease furin. [7] The crystal structure of core gp120 shows an organization with an outer domain, an inner domain with respect to its termini and a bridging sheet.
A schematic structure of a HIV-1 protease. The monomers are shown in green and cyan, the Asp-25 and Asp-25´ residues are shown in red, and Ile50 and Ile50´ residues linked to a water molecule are shown in purple. The HIV protease is a C2-symmetric homodimeric enzyme consisting of two 99 amino acid monomers.
In molecular biology, Tat is a protein that is encoded for by the tat gene in HIV-1. [1] [2] Tat is a regulatory protein that drastically enhances the efficiency of viral transcription. [2] Tat stands for "Trans-Activator of Transcription". The protein consists of between 86 and 101 amino acids depending on the subtype. [3]
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