1H, 13C and 15N resonance assignment of the anti-HIV lectin from Oscillatoria 
agardhii.

Carneiro, M. G.; Koharudin, L. M.; Griesinger, C.; Gronenborn, A. M.; Lee, D.

doi:10.1007/s12104-015-9600-8

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1H, 13C and 15N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii.

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Carneiro, M. G.
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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Citation

Carneiro, M. G., Koharudin, L. M., Griesinger, C., Gronenborn, A. M., & Lee, D. (2015). 1H, 13C and 15N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii. Biomolecular NMR Assignments, 9(2), 317-319. doi:10.1007/s12104-015-9600-8.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0026-C70F-5

Abstract

Lectins from different sources are known to interfere with HIV infection. The anti-viral activity is mediated by binding to high mannose sugars present on the viral envelope, thereby inhibiting cell entry. The lectin from Oscillatoria agardhii agglutinin (OAA) specifically recognizes a unique substructure of high mannose sugars and exhibits broad anti-HIV activity. Here we report the assignment of backbone and side-chain (1)H, (13)C and (15)N resonances of free OAA. 1H, 13C and 15N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii - ResearchGate. Available from: http://www.researchgate.net/publication/272297497_1H_13C_and_15N_resonance_assignment_of_the_anti-HIV_lectin_from_Oscillatoria_agardhii [accessed May 5, 2015].