Proteopedia - User contributions [en]

Crixivan

2016-12-06T06:09:01Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==

<StructureSection load='2b7z' size='340' side='right' caption='Crixivan molecule and structure of HIV-1 protease bound to Crixivan, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene='74/745991/Crixivan/2'>

==Structure==
Crixivan, 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-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 ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

Crixivan

2016-12-06T05:55:57Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==

<StructureSection load='2b7z' size='340' side='right' caption='Crixivan molecule and structure of HIV-1 protease bound to Crixivan, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' 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 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-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 ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T05:44:47Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==

<StructureSection load='2b7z' size='340' side='right' caption='Crixivan molecule and structure of HIV-1 protease bound to Crixivan, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' 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 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-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 ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T03:16:00Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==

<StructureSection load='2b7z' size='340' side='right' caption='Crixivan molecule and structure of HIV-1 protease bound to crixivan, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' 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 conforms the molecule to the active site. The hydroxyethylene group stabilizes the molecule and prevents lysis.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T03:09:33Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==

<StructureSection load='2b7z' size='340' side='right' caption='Crixivan molecule and structure of HIV-1 protease bound to crixivan, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' 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.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T03:05:19Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==

<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' 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.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T02:37:04Z

Kerry Frattarola:

==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.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T02:33:07Z

Kerry Frattarola:

==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 doesn't lyse due to the molecule's stability.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T02:28:24Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="74/745991/Crixivan/2" align="right" caption="Crixivan molecule ([[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 doesn't lyse due to the molecule's stability.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T02:18:44Z

Kerry Frattarola:

<applet load="" size="350" color="" frame="true" spin="on" Scene ="74/745991/Crixivan/2" align="right" caption="Crixivan molecule ([[1hsg]])"/>
==Human Immunodeficiency Virus protease inhibitor==

==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 doesn't lyse due to the molecule's stability.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T02:15:08Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="74/745991/Crixivan/2" align="right" caption="Crixivan molecule ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 doesn't lyse due to the molecule's stability.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.<ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings.<ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:57:22Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:56:08Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:51:57Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:48:06Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:46:41Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:43:28Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:41:19Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[https://upload.wikimedia.org/wikipedia/commons/0/00/Aspartyl_protease_mechanism.png]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:38:48Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:38:08Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

<<https://en.wikipedia.org/wiki/Aspartic_protease#/media/File:Aspartyl_protease_mechanism.png>>

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:25:29Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<applet load="" size="350" color="" frame="true" spin="on" Scene ="Indinavir/Indinavir/1" align="right" caption="Crixivan, also known as Indinavir, ([[1hsg]])"/>

==Structure==
[[Crixivan]], 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The amide is attacked by the Asp25 of the protease, however the peptide bond doesn't lyse due to the stability of the molecule.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T01:09:01Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
[[Crixivan]] is an antiviral compound that acts as a protease inhibitor. The drug 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 group on Crixivan interacts with Arg8 in the protease to conform Crixivan to the active site. The ketone is attacked by the Asp25 of the protease, forming a bond between the ketone and amide that doesn't lyse due to the nature of the inhibitor.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-06T00:58:53Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
[[Crixivan]] is an antiviral compound that acts as a protease inhibitor. The drug 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 group on Crixivan interacts with Arg8 in the protease to conform Crixivan to the active site. The ketone is attacked by with the Asp25 of the protease, forming a bond between the ketone and amide that doesn't lyse due to the nature of the inhibitor.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-05T22:07:44Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
[[Crixivan]] is an antiviral compound that acts as a protease inhibitor. The drug 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 group on Indinavir interacts with Arg8 in the protease to conform Indinavir to the active site. The ketone is attacked by with the Asp25 of the protease, forming a bond between the ketone and amide doesn't lyse due to the nature of the inhibitor.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The <scene name='74/745991/Progress/2'>active site</scene> of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-05T21:39:32Z

Kerry Frattarola:

<scene name='74/745991/Progress/2'>TextToBeDisplayed</scene>
==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
[[Crixivan]] is an antiviral compound that acts as a protease inhibitor. Figure 2 below depicts Crixivan’s structure. The drug 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. Crixivan’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The active site of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-05T21:27:53Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
[[Crixivan]] is an antiviral compound that acts as a protease inhibitor. Figure 2 below depicts Crixivan’s structure. The drug 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. Crixivan’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The active site of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-05T20:41:20Z

Kerry Frattarola:

==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='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
Crixivan is an antiviral compound that acts as a protease inhibitor. Figure 2 below depicts Crixivan’s structure. The drug 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. Crixivan’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== 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 polyproteins, 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 polypeptides containing multiple proteins 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>

== Mechanism ==
The active site of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivan's pyridine ring and the interactions between Gly27 and Crixivan's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Crixivan blocks the cleavage of the Gag multi-protein peptide. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-12-05T03:50:02Z

Kerry Frattarola:

==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='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibitor. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polypeptides containing multiple proteins 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 Indinavir 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>

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-17T11:21:31Z

Kerry Frattarola:

==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='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibitor. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir 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>

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell-to-cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-17T11:16:59Z

Kerry Frattarola:

==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='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir increased the potency of the drug compared to earlier protease inhibiters. <ref name="Antimicrobial">Scholar, E. M., & Pratt, W.B. (2000). ''The Antimicrobial Drugs'' (2nd ed.). New York, NY: Oxford University Press.</ref>

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. <ref>DOI:10.1111/j.1432-1033.2004.04060.x</ref> This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.<ref name="Antimicrobial" />

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-17T11:02:47Z

Kerry Frattarola:

==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='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir increased the potency of the drug compared to earlier protease inhibiters.

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.<ref>Scholar, E. M., & Pratt, W.B. (2000). ''The Antimicrobial Drugs'' (2nd ed.). New York, NY: Oxford University Press.</ref>

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-17T02:48:35Z

Kerry Frattarola:

==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='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir increased the potency of the drug compared to earlier protease inhibiters.

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.<ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.<ref>Pratt, W. B., Scholar, E. M. (2000). The Antimicrobial Drugs. p. 570
Oxford University Press, 2000 (idk this is the wrong format i tried)</ref>

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-17T02:19:15Z

Kerry Frattarola:

==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='Structure of HIV-1 protease bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir increased the potency of the drug compared to earlier protease inhibiters.

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25. <ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-17T01:59:21Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir increased the potency of the drug compared to earlier protease inhibiters.

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. <ref>PMID:11410934</ref> Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25. <ref>DOI:10.1002/rmv.624</ref> The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. This blocks all further cleavage of viral peptides by the protease molecule.

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T23:18:52Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins, 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir increased the potency of the drug compared to earlier protease inhibiters.

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. (Don't know how to reference this) Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25. The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. This blocks all further cleavage of viral peptides by the protease molecule.

Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T23:16:08Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==
Indinavir functions as a competitive inhibitor affecting the HIV protease protein. Indinavir 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 polyproteins 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 polyproteins into vital proteins such as reverse transcriptase, integrase, and protease. The virus will halt development if the polyproteins 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 Indinavir increased the potency of the drug compared to earlier protease inhibiters.

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. (Don't know how to reference this) Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25. The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. This blocks all further cleavage of viral peptides by the protease molecule.

Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T19:03:19Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. (Don't know how to reference this) Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the transition state of Gag protein peptides. The virus' peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis. Indinavir contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25. The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Indinavir's pyridine ring and the interactions between Gly27 and Indinavir's aromatic rings. This blocks all further cleavage of viral peptides by the protease molecule.

Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==
Indinavir blocks the cleavage of the Gag polyprotein. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T18:00:24Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. Its ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==

== Mechanism ==
The active site of HIV-1 protease is inhibited by Indinavir when the molecule interacts with the specific sites that a viral protein normally would interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site. (Don't know how to reference this) Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Indinavir molecule enters the protease active site it imitates the specific protein. I wrote something but can't remember what it was.

Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==
Indinavir blocks the cleavage of gag and gag-pol proteins. This inhibition does not allow for the maturation of new viral particles produced from infected cells. Viral particles that do not mature will not be able to infect new cells, lowering the viral load. Protease inhibitors do not have any effect on already infected cells but they do prevent further cell to cell transmission of the virus.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T04:08:06Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. It's ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==

== Mechanism ==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T04:04:38Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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. Indinavir’s pyridine attracts protease Arg8 to hold it in place. It's ketone interacts with the protease Asp25 to perform initiate aspartic catalysis. The bond between the ketone and amine doesn't lyse due to the nature of the inhibitor.

== Function ==

== Mechanism ==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T03:51:21Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug 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>. Indinavir 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 Arginine in the protease interacts with Indinavir’s pyridine to hold it in place. The hydroxyl groups off the cyclopentanes, ketone and amide interact with the Asp25 of HIV-1 protease to perform catabolism (1).

== Function ==

== Mechanism ==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T03:45:48Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==

== Function ==

== Mechanism ==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T03:29:20Z

Kerry Frattarola:

==Human Immunodeficiency Virus protease inhibitor==
<StructureSection load='2b7z' size='340' side='right' caption='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir is an antiviral compound that acts as a protease inhibiter. Figure 2 below depicts Indinavir’s structure. The drug has a molecular weight of 711.875 g/mol and is very soluble in water and ethanol. Indinavir 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 Arginine in the protease interacts with Indinavir’s pyridine to hold it in place. The hydroxyl groups off the cyclopentanes, ketone and amide interact with the Asp25 of HIV-1 protease to perform catabolism (1).

== Function ==

== Mechanism ==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T03:02:23Z

Kerry Frattarola:

User:Kerry Frattarola/Sandbox 1

2016-11-16T03:00:05Z

Kerry Frattarola:

==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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==

== Function ==

== Mechanism ==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T02:53:18Z

Kerry Frattarola:

User:Kerry Frattarola/Sandbox 1

2016-11-16T02:51:26Z

Kerry Frattarola:

==Crixivan==
<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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==

== Function ==

== Mechanism ==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Cellular Effects ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T02:50:21Z

Kerry Frattarola:

==Crixivan==
<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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Function ==

== Mechanism ==

== Cellular Effects ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T02:45:42Z

Kerry Frattarola:

<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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Crixivan==

==Structure==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Function ==

== Mechanism ==

== Cellular Effects ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

User:Kerry Frattarola/Sandbox 1

2016-11-16T02:31:48Z

Kerry Frattarola:

==Crixivan==
<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='Structure of HIV-1 protease mutant bound to indinavir, ([[2b7z]]), [[Resolution|resolution]] 2.20Å' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

==Structure==
Indinavir acts with the Asp25, Thr26 and Gly27 subunits in the HIV-1 protease enzyme.<ref>PMID:11410934</ref>

== Function ==

== Mechanism ==

== Cellular Effects ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>