Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9139120 | Journal of Structural Biology | 2005 | 6 Pages |
Abstract
The monoclonal antibody 1696, elicited by HIV-1 protease, inhibits the activity of both HIV-1 and HIV-2 proteases with inhibition constants in the low nanomolar range. The antibody cross-reacts with peptides derived from the N-terminal region of both proteases. The crystal structure of the recombinant single-chain Fv fragment of 1696 complexed with an N-terminal peptide from the HIV-2 protease has been determined at 1.88Â Ã
resolution. Interactions of the peptide with scFv1696 are compared with the previously reported structure of scFv1696 in complex with the corresponding peptide from HIV-1 protease. The origin of cross-reactivity of mAb1696 with HIV proteases is discussed.
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Authors
Pavlina Rezacova, Jiri Brynda, Julien Lescar, Milan Fabry, Magda Horejsi, Irena Sieglova, Juraj Sedlacek, Graham A. Bentley,