HIV-1 Protease
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
Product Specs
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMNLPG RWKPKMIGGI GGFIKVRQYD QILIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNF.
Product Science Overview
HIV-1 protease is a crucial enzyme in the life cycle of the Human Immunodeficiency Virus type 1 (HIV-1), the virus responsible for Acquired Immunodeficiency Syndrome (AIDS). This enzyme is essential for the maturation of viral particles, making it a key target for antiretroviral therapy. The recombinant form of HIV-1 protease has been extensively studied to understand its structure, function, and role in drug resistance.
The first high-resolution structure of HIV-1 protease was published in 1989 by scientists at Merck Sharp and Dohme Research Laboratories. They used recombinant protease expressed in bacteria, which revealed essential features of the enzyme’s catalytic apparatus . This breakthrough paved the way for the development of protease inhibitors, a class of antiretroviral drugs that have significantly improved the management of HIV/AIDS.
HIV-1 protease is a homodimeric enzyme belonging to the aspartate family, also known as aspartyl retropepsin . It plays a crucial role in the viral maturation process by cleaving the Gag and Gag-Pol polyproteins into functional viral proteins. This cleavage is essential for the assembly of mature, infectious viral particles.
Recombinant HIV-1 protease is produced using genetic engineering techniques, where the protease gene is cloned and expressed in a suitable host, such as bacteria. This allows for the production of large quantities of the enzyme for research purposes. The recombinant form retains the same structural and functional properties as the native enzyme, making it an invaluable tool for studying the enzyme’s characteristics and interactions with inhibitors.
The structural insights gained from studying recombinant HIV-1 protease have been instrumental in the development of protease inhibitors. These drugs bind to the active site of the enzyme, preventing it from cleaving the viral polyproteins and thereby inhibiting viral replication. However, the high mutation rate of HIV-1 leads to the emergence of drug-resistant strains. Understanding the impact of individual protease mutations on drug susceptibility is crucial for developing more effective therapies .
