Sandbox Reserved 1735: Difference between revisions
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{{Sandbox_Reserved_Kim_Lane}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_Kim_Lane}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==HIV Protease== | ==HIV Protease== | ||
<StructureSection load=' | <StructureSection load='3qaa' size='340' side='right' caption='HIV-1 Protease PDB 3hvp' scene=''> | ||
==Introduction== | ==Introduction== | ||
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== Structural Highlights of HIV-1 protease== | == Structural Highlights of HIV-1 protease== | ||
There are hundreds of forms of HIV-1 protease. The basic HIV-1 protease contains two subunits that are dimers. These subunits contain an alpha helix, 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 dimer is the active site | There are hundreds of forms of HIV-1 protease. The basic HIV-1 protease contains two subunits that are dimers. These subunits contain an alpha helix, 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 dimer is the active site. Mutants have different molecules bound to the active site, making different mutants of HIV-1 protease. Some mutants are more easily controlled by drugs, such as protease inhibitors, while other mutations 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. The HIV-1 protease shown is a wild-type protease. [[Immunodeficiency virus protease]] | ||
==Structural Highlights of HIV-2 protease== | ==Structural Highlights of HIV-2 protease== | ||
