Sampling of Glycan-Bound Conformers by the Anti-HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar
2015 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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Sampling of Glycan-Bound Conformers by the Anti-HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar
Carneiro, M. G. ; Koharudin, L. M. I.; Ban, D. ; Sabo, T. M. ; Trigo-Mourino, P. ; Mazur, A. & Griesinger, C. et al. (2015)
Angewandte Chemie International Edition, 54(22) pp. 6462-6465. DOI: https://doi.org/10.1002/anie.201500213
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- Authors
- Carneiro, Marta G. ; Koharudin, Leonardus M. I.; Ban, David ; Sabo, T. Michael ; Trigo-Mourino, Pablo ; Mazur, Adam ; Griesinger, Christian ; Gronenborn, Angela M.; Lee, Donghan
- Abstract
- Lectins from different sources have been shown to interfere with HIV infection by binding to the sugars of viral-envelope glycoproteins. Three-dimensional atomic structures of a number of HIV-inactivating lectins have been determined, both as free proteins and in glycan-bound forms. However, details on the mechanism of recognition and binding to sugars are elusive. Herein we focus on the anti-HIV lectin OAA from Oscillatoria agardhii: We show that in the absence of sugars in solution, both the sugar-free and sugar-bound protein conformations that were observed in the X-ray crystal structures exist as conformational substates. Our results suggest that glycan recognition occurs by conformational selection within the ground state; this model differs from the popular excited-state model. Our findings provide further insight into molecular recognition of the major receptor on the HIV virus by OAA. These details can potentially be used for the optimization and/or development of preventive anti-HIV therapeutics.
- Issue Date
- 2015
- Journal
- Angewandte Chemie International Edition
- ISSN
- 1433-7851
- eISSN
- 1521-3773
- Language
- English