User:Kerry Frattarola/Sandbox 1: Difference between revisions

(3 intermediate revisions by the same user not shown)

Line 1:

==Human Immunodeficiency Virus protease inhibitor==

<~~applet~~ load="" size=~~"350" color~~=~~"" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="~~right" caption=~~"Indinavir, better known as~~ Crixivan, ([[~~1hsg~~]])"/>

==Structure==

<scene name='74/745991/Crixivan/2'>Crixivan</scene>, also known as [[Indinavir]], is an antiviral compound that acts as a protease inhibitor. The <scene name='74/745991/Crixivan/2'>structure</scene> has a molecular weight of 711.875 g/mol and is very soluble in water and ethanol.<ref>Physicians Desk Reference 66th ed. PDR Network, LLC, Montvale, NJ. p. 2086 (2012)</ref> Crixivan works by specifically binding to the HIV-1 protease active site by mimicking a target substrate protein and essentially becoming “stuck” in the enzyme active site, disabling the enzyme. The pyridine ring on Crixivan ~~interacts with Arg8 in~~ the ~~protease to conform~~ to the active site. ~~When the HIV-1 protease attacks the~~ hydroxyethylene group ~~of the molecule, the bond does not lyse due to~~ the molecule~~'s stability~~.

<scene name='74/745991/Crixivan/2'>Crixivan</scene>, also known as [[Indinavir]], is an antiviral compound that acts as a protease inhibitor. The <scene name='74/745991/Crixivan/2'>structure</scene> has a molecular weight of 711.875 g/mol and is very soluble in water and ethanol.<ref>Physicians Desk Reference 66th ed. PDR Network, LLC, Montvale, NJ. p. 2086 (2012)</ref> Crixivan works by specifically binding to the HIV-1 protease active site by mimicking a target substrate protein and essentially becoming “stuck” in the enzyme active site, disabling the enzyme. The pyridine ring on Crixivan conforms the molecule to the active site. The hydroxyethylene group stabilizes the molecule and prevents cleavage.

== Function ==

Crixivan functions as a competitive inhibitor affecting the HIV protease protein. Crixivan ~~essentially~~ mimics the target substrate of HIV protease and binds to the protease active site. The HIV protease enzyme is essential to the reproduction of the HIV virus and further infection. HIV protease performs post-translational cleavage of multi-protein peptides, such as Gag, that serve as important factors in virus development. HIV protease is released from the ~~virus~~ soon after the cell is infected and immediately ~~beings lysing~~ the multi-protein peptides into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polypeptides are not ~~lysed~~ and the resulting particles from the virus will be non-infective. The hydrophobic phenyl functional groups located on the terminal ends of Crixivan ~~increased~~ the potency of the drug compared to earlier protease inhibitors.<ref name="Antimicrobial">Scholar, E. M., & Pratt, W.B. (2000). ''The Antimicrobial Drugs'' (2nd ed.). New York, NY: Oxford University Press.</ref>

Crixivan functions as a competitive inhibitor affecting the HIV-1 protease protein. Crixivan mimics the target substrate of the HIV protease and binds to the protease active site. The HIV protease enzyme is essential for the reproduction of the HIV virus and further infection. HIV protease performs post-translational cleavage of multi-protein peptides, such as the Gag protein, that serve as important factors in virus development. HIV protease is released from the viral particle soon after the cell is infected and immediately begins cleaving the multi-protein peptides into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polypeptides are not cleaved and the resulting particles from the virus will be non-infective. The hydrophobic phenyl functional groups located on the terminal ends of Crixivan increase the potency of the drug compared to earlier protease inhibitors.<ref name="Antimicrobial">Scholar, E. M., & Pratt, W.B. (2000). ''The Antimicrobial Drugs'' (2nd ed.). New York, NY: Oxford University Press.</ref>

== Mechanism ==

@@ Line 1: / Line 1: @@
 ==Human Immunodeficiency Virus protease inhibitor==
-<applet   load="" size="350" color="" frame="true"  spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Indinavir, better known as Crixivan, ([[1hsg]])"/>
+<StructureSection load='2b7z' size='340' side='right' caption='Crixivan molecule and structure of HIV-1 protease bound to Crixivan, ([[2b7z]]), [[Resolution|resolution]] 2.20&Aring;' scene='74/745991/Crixivan/2'>
 ==Structure==
-<scene name='74/745991/Crixivan/2'>Crixivan</scene>, also known as [[Indinavir]], is an antiviral compound that acts as a protease inhibitor. The <scene name='74/745991/Crixivan/2'>structure</scene> has a molecular weight of 711.875 g/mol and is very soluble in water and ethanol.<ref>Physicians Desk Reference 66th ed. PDR Network, LLC, Montvale, NJ. p. 2086 (2012)</ref> Crixivan works by specifically binding to the HIV-1 protease active site by mimicking a target substrate protein and essentially becoming “stuck” in the enzyme active site, disabling the enzyme. The pyridine ring on Crixivan interacts with Arg8 in the protease to conform to the active site. When the HIV-1 protease attacks the hydroxyethylene group of the molecule, the bond does not lyse due to the molecule's stability.
+<scene name='74/745991/Crixivan/2'>Crixivan</scene>, also known as [[Indinavir]], is an antiviral compound that acts as a protease inhibitor. The <scene name='74/745991/Crixivan/2'>structure</scene> has a molecular weight of 711.875 g/mol and is very soluble in water and ethanol.<ref>Physicians Desk Reference 66th ed. PDR Network, LLC, Montvale, NJ. p. 2086 (2012)</ref> Crixivan works by specifically binding to the HIV-1 protease active site by mimicking a target substrate protein and essentially becoming “stuck” in the enzyme active site, disabling the enzyme. The pyridine ring on Crixivan conforms the molecule to the active site. The hydroxyethylene group stabilizes the molecule and prevents cleavage.
 == Function ==
-Crixivan functions as a competitive inhibitor affecting the HIV protease protein. Crixivan essentially mimics the target substrate of HIV protease and binds to the protease active site. The HIV protease enzyme is essential to the reproduction of the HIV virus and further infection. HIV protease performs post-translational cleavage of multi-protein peptides, such as Gag, that serve as important factors in virus development. HIV protease is released from the virus soon after the cell is infected and immediately beings lysing the multi-protein peptides into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polypeptides are not lysed and the resulting particles from the virus will be non-infective. The hydrophobic phenyl functional groups located on the terminal ends of Crixivan increased the potency of the drug compared to earlier protease inhibitors.<ref name="Antimicrobial">Scholar, E. M., & Pratt, W.B. (2000). ''The Antimicrobial Drugs'' (2nd ed.). New York, NY: Oxford University Press.</ref>
+Crixivan functions as a competitive inhibitor affecting the HIV-1 protease protein. Crixivan mimics the target substrate of the HIV protease and binds to the protease active site. The HIV protease enzyme is essential for the reproduction of the HIV virus and further infection. HIV protease performs post-translational cleavage of multi-protein peptides, such as the Gag protein, that serve as important factors in virus development. HIV protease is released from the viral particle soon after the cell is infected and immediately begins cleaving the multi-protein peptides into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polypeptides are not cleaved and the resulting particles from the virus will be non-infective. The hydrophobic phenyl functional groups located on the terminal ends of Crixivan increase the potency of the drug compared to earlier protease inhibitors.<ref name="Antimicrobial">Scholar, E. M., & Pratt, W.B. (2000). ''The Antimicrobial Drugs'' (2nd ed.). New York, NY: Oxford University Press.</ref>
 == Mechanism ==