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== Structural Highlights of HIV-1 protease==

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. ~~<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>. This structure highlighted to the right is a wild type of HIV-1 protease, PDB code ~~1dvs~~. Notice in this wild type, there are molecules bound to the active site. This 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. In the mutant 3hvp molecules are not bound at the active site. ~~<Structure load='3hvp' size='250' frame='true' align='right' caption='HIV-1 PR mutant' scene='3hvp mutant' />~~ 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]]

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]]

==Structural Highlights of HIV-2 protease==

Sandbox Reserved 1735: Difference between revisions

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 == Structural Highlights of HIV-1 protease==
-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. <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>. This structure highlighted to the right is a wild type of HIV-1 protease, PDB code 1dvs. Notice in this wild type, there are molecules bound to the active site. This 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. In the mutant 3hvp molecules are not bound at the active site. <Structure load='3hvp' size='250' frame='true' align='right' caption='HIV-1 PR mutant' scene='3hvp mutant' /> 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]]
+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]]
 ==Structural Highlights of HIV-2 protease==