The Preserved HTH-Docking Cleft of HIV-1 Integrase Is Functionally Critical

• Published in: Structure (London) Vol. 24; no. 11; pp. 1936 - 1946
• Main Authors: Galilee, Meytal, Britan-Rosich, Elena, Griner, Sarah L., Uysal, Serdar, Baumgärtel, Viola, Lamb, Don C., Kossiakoff, Anthony A., Kotler, Moshe, Stroud, Robert M., Marx, Ailie, Alian, Akram
• Format: Journal Article
• Language: English
• Published: United States Elsevier Ltd 01.11.2016
• Subjects: Catalytic Domain; Crystallography, X-Ray; Helix-Turn-Helix Motifs; HIV Integrase - chemistry; HIV Integrase - genetics; HIV Integrase - metabolism; HIV-1 - chemistry; HIV-1 - enzymology; Models, Molecular; Molecular Docking Simulation; Protein Binding; Protein Multimerization; Protein Structure, Secondary; RNA, Viral - metabolism

HIV-1 integrase (IN) catalyzes viral DNA integration into the host genome and facilitates multifunctional steps including virus particle maturation. Competency of IN to form multimeric assemblies is functionally critical, presenting an approach for anti-HIV strategies. Multimerization of IN depends...