Sandbox Reserved 1735: Difference between revisions

There are hundreds of forms of HIV-1 protease. The basic HIV-1 protease contains two subunits that are homodimers [10]. These subunits contain beta sheets running antiparallel to each other, and random coils. <scene name='91/919044/Chain_a/1'>This is a subunit of HIV-1 protease PDB 3hvp.</scene> The beta sheets are in a jelly roll fold conformation. In the middle of the homodimer is the active site. Below the active site are the catalytic aspartates. <scene name='91/919044/Catalytic_aspartase/1'>Catalytic Aspartates.</scene> At the bottom of the molecule is the <scene name='91/919044/Dimerization_regions/1'>dimerization region</scene>. Different mutants and wild types have different molecules bound to the active site, making different versions of HIV-1 protease. Some versions are more easily controlled by drugs, such as protease inhibitors, while other versions are more drug-resistant. It is difficult to determine which form of HIV-1 protease a person has, and each case of HIV-1 has to be treated on a case basis because there are so many mutants and wild types [10]. [[Immunodeficiency virus protease]]

Due to the nature of HIV, many drug-resistant variants occur. Every time a new patient is infected with HIV, there is a chance that a new HIV protease mutation will arise. It is important that society and scientists remain vigilant in the fight against HIV. Mutations in the HIV-1 and HIV-2 proteases lead to drug resistance to HIV. [11].  

10. Venkatakrishnan, B.; Palii, M.-L.; Agbandje-McKenna, M. Mining the protein data bank to differentiate error from structural variation in clustered static structures: An examination of HIV protease. Viruses 2012, 4(3), 348-362.

 

11. Weber, I. T.; Wang, Y.-F.; Harrison, R. W. HIV Protease: Historical Perspective and Current Research. Viruses 2021, 13 (5), 839.