Sandbox Reserved 1735: Difference between revisions

Line 9:

== 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. The full image of the PDB 3hvp represents the dimer of HIV-1 protease. 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. This particular mutant, PBD 3hvp, is ~~bound~~ drug resistant.

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. The full image of the PDB 3hvp represents the dimer of HIV-1 protease. 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. This particular mutant, PBD 3hvp, is drug resistant.

Sandbox Reserved 1735: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 07:12, 15 November 2022 view source Jynna Harrell (talk \| contribs) 57 edits No edit summary ← Older edit		Revision as of 07:12, 15 November 2022 view source Jynna Harrell (talk \| contribs) 57 edits No edit summary Newer edit →
Line 9:		Line 9:
	== 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. The full image of the PDB 3hvp represents the dimer of HIV-1 protease. 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. This particular mutant, PBD 3hvp, is ~~bound~~ drug resistant.		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. The full image of the PDB 3hvp represents the dimer of HIV-1 protease. 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. This particular mutant, PBD 3hvp, is drug resistant.