Sandbox Reserved 1735: Difference between revisions

<StructureSection load='1d4s' size='340' side='right' caption='HIV-1 Protease PDB 1d4s' scene=''>

There are hundreds of forms of HIV-1 proteases. 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. 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. At the bottom of the molecule is the <scene name='91/919044/Dimerization_regions/1'>dimerization region</scene>. This structure highlighted to the right is a wild type of HIV-1 protease, PDB code 1d4s. Notice in this wild type, there are molecules bound to the active site. This HIV-1 protease, 1d4s, is a wild type with catalytic aspartates, a flap domain, an elbow, and a core domain [10]. In other mutant forms, molecules are bound to other regions than the active site. In the mutant <scene name='91/919044/Mutant/1'> 3hvp</scene> molecules are not bound at the active site. 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]]