Sandbox 645: Difference between revisions

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=='''Introduction'''==

HIV -1 protease (HIV PR ) is a retroviral aspartyl protease that is derived from HIV-1, a lentivirus that is best characterized for its ability to lower host immunity by infecting CD4+ T lymphocytes, macrophages, and dendritic cells. Aspartyl proteases are protease enzymes that utilize aspartate residue(s) for the catalysis of peptide substrates. Eukaryotic forms of these proteases include the pepsins, cathepsins and renins. While they have a two-domain structure, the retroviral aspartyl proteases are much smaller as homologous to a single domain of the eukaryotic aspartic proteases. Unlike most members of the aspartyl protease class, which generally exist as two domain monomers, HIV protease is a dimmer with two identical subunits that are comprised of 99 amino acids. The HIV PR, together with single stranded RNA (ssRNA), reverse transcriptase, integrase, and other viral factors, is found inside the HIV-1 virion. As an important viral protein, it plays a crucial role in successful viral propagation.

HIV -1 protease (HIV PR ) is a retroviral aspartyl protease that is derived from HIV-1, a lentivirus that is best characterized for its ability to lower host immunity by infecting CD4+ T lymphocytes, macrophages, and dendritic cells. Aspartyl proteases are protease enzymes that utilize aspartate residue(s) for the catalysis of peptide substrates. Eukaryotic forms of these proteases include the pepsins, cathepsins and renins. While they have a two-domain structure, the retroviral aspartyl proteases are much smaller and homologous to a single domain of the eukaryotic aspartic proteases. Unlike most members of the aspartyl protease class, which generally exist as two domain monomers, HIV protease is a dimmer with two identical subunits that are comprised of 99 amino acids. The HIV PR, together with single stranded RNA (ssRNA), reverse transcriptase, integrase, and other viral factors, is found inside the HIV-1 virion. As an important viral protein, it plays a crucial role in successful viral propagation.

Sandbox 645: Difference between revisions

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Revision as of 04:38, 27 November 2012 view source Charles Short (talk \| contribs) 89 edits No edit summary ← Older edit		Revision as of 04:58, 27 November 2012 view source Charles Short (talk \| contribs) 89 edits No edit summary Newer edit →
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	=='''Introduction'''==		=='''Introduction'''==
	HIV -1 protease (HIV PR ) is a retroviral aspartyl protease that is derived from HIV-1, a lentivirus that is best characterized for its ability to lower host immunity by infecting CD4+ T lymphocytes, macrophages, and dendritic cells. Aspartyl proteases are protease enzymes that utilize aspartate residue(s) for the catalysis of peptide substrates. Eukaryotic forms of these proteases include the pepsins, cathepsins and renins. While they have a two-domain structure, the retroviral aspartyl proteases are much smaller as homologous to a single domain of the eukaryotic aspartic proteases. Unlike most members of the aspartyl protease class, which generally exist as two domain monomers, HIV protease is a dimmer with two identical subunits that are comprised of 99 amino acids. The HIV PR, together with single stranded RNA (ssRNA), reverse transcriptase, integrase, and other viral factors, is found inside the HIV-1 virion. As an important viral protein, it plays a crucial role in successful viral propagation.		HIV -1 protease (HIV PR ) is a retroviral aspartyl protease that is derived from HIV-1, a lentivirus that is best characterized for its ability to lower host immunity by infecting CD4+ T lymphocytes, macrophages, and dendritic cells. Aspartyl proteases are protease enzymes that utilize aspartate residue(s) for the catalysis of peptide substrates. Eukaryotic forms of these proteases include the pepsins, cathepsins and renins. While they have a two-domain structure, the retroviral aspartyl proteases are much smaller and homologous to a single domain of the eukaryotic aspartic proteases. Unlike most members of the aspartyl protease class, which generally exist as two domain monomers, HIV protease is a dimmer with two identical subunits that are comprised of 99 amino acids. The HIV PR, together with single stranded RNA (ssRNA), reverse transcriptase, integrase, and other viral factors, is found inside the HIV-1 virion. As an important viral protein, it plays a crucial role in successful viral propagation.