title: (1)H, (13)C and (15)N resonance assignment of the anti-HIV lectin from Oscillatoria agardhii.
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.
authors: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
authors: Marta G
authors: MG
authors: Carneiro
authors: Department of Structural Biology, University of Pittsburgh School of Medicine, 1050 Biomedical Science Tower 3, 3501 5th Ave, Pittsburgh, PA, 15260, USA.
authors: Leonardus M I
authors: LM
authors: Koharudin
authors: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
authors: Christian
authors: C
authors: Griesinger
authors: Department of Structural Biology, University of Pittsburgh School of Medicine, 1050 Biomedical Science Tower 3, 3501 5th Ave, Pittsburgh, PA, 15260, USA.
authors: Angela M
authors: AM
authors: Gronenborn
authors: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany. dole@nmr.mpibpc.mpg.de.
authors: Donghan
authors: D
authors: Lee
mesh_terms: D066241:Carbon-13 Magnetic Resonance Spectroscopy; D037102:Lectins / Q000737:chemistry*; D009587:Nitrogen Isotopes; D054300:Oscillatoria / Q000737:chemistry*; D017433:Protein Structure, Secondary; D066244:Proton Magnetic Resonance Spectroscopy
chemical_list: D037102:Lectins; D009587:Nitrogen Isotopes
keywords: Anti-HIV lectins; NMR assignment; Oscillatoria agardhii agglutinin