The E. coli derived 36 kDa recombinant protein is a non-glycosylated polypeptide chain, containing the HIV-1 immunodominant regions from the pol protein (intergrase) and fused with a six histidines tag.
Integrase is an enzyme produced by the HIV which enables its genetic material to be integrated into the DNA of the infected cell and is a key component in the pre-integration complex. HIV integrase contains 3 domains, an N-terminal HH-CC zinc fingerdomainwhich is partially responsible for multimerization, a central catalytic domain and a C-terminal domain. Both Central catalytic domain and C-terminal domains have been shown to bind both viral and cellular DNA. No crystal structure data exists with Integrase bound to its DNA substrates. HIV-1 integrase functions as a dimeror a tetramer. Additionally, several host cellular proteins interact with integrase and may facilitate the integration process.
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