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Journal Article

Sampling of glycan-bound conformers by the anti-HIV lectin Oscillatoria agardhii agglutinin in the absence of sugar.

MPS-Authors
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Carneiro,  M. G.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Ban,  D.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Sabo,  T. M.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Trigo-Mourino,  P.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Mazur,  A.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lee,  D.
Department of NMR-based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Supplementary Material (public)

2149631_Suppl.pdf
(Supplementary material), 3MB

Citation

Carneiro, M. G., Koharudin, L. M., Ban, D., Sabo, T. M., Trigo-Mourino, P., Mazur, A., et al. (2015). Sampling of glycan-bound conformers by the anti-HIV lectin Oscillatoria agardhii agglutinin in the absence of sugar. Angewandte Chemie International Edition, 54(22), 6462-6465. doi:10.1002/anie.201500213.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0026-C6EC-A
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.