Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease

Chun Tang, John M. Louis, Annie Aniana, Jeong-Yong Suh and G. Marius Clore ()
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Chun Tang: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA
John M. Louis: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA
Annie Aniana: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA
Jeong-Yong Suh: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA
G. Marius Clore: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA

Nature, 2008, vol. 455, issue 7213, 693-696

Abstract: HIV-1 protease unmasked The HIV-1 protease enzyme is indispensable for viral maturation, making it a major potential target of anti-HIV therapy. Its role is to split newly formed Gag and Gag-Pol polyproteins to produced finished structural and functional proteins — itself included. The early events in the autoprocessing of HIV-1 protease, in which a precursor dimer is thought to undergo intramolecular cleavage, have now been visualized using NMR spectroscopy and paramagnetic relaxation enhancement. This reveals that although primarily monomeric, the protease is also present as transient encounter complexes that occupy a wide range of orientations relative to the mature dimer. The N-terminal region makes transient intra- and intersubunit contacts with the substrate binding site, allowing autocleavage to occur when the correct dimer orientation is sampled by the encounter complex.

Date: 2008
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DOI: 10.1038/nature07342

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