2MWH
NMR solution structure of ligand-free OAA
Summary for 2MWH
| Entry DOI | 10.2210/pdb2mwh/pdb |
| NMR Information | BMRB: 25324 |
| Descriptor | Anti-HIV lectin OAA (1 entity in total) |
| Functional Keywords | protein binding, sugar binding protein-antiviral protein complex, sugar binding protein/antiviral protein |
| Biological source | Planktothrix agardhii |
| Total number of polymer chains | 1 |
| Total formula weight | 13930.76 |
| Authors | Lee, D.,Carneiro, M.G.,Koharudin, L.M.,Griesinger, C.,Gronenborn, A.M.,Ban, D.,Sabo, T.,Trigo-Mourino, P.,Mazur, A. (deposition date: 2014-11-10, release date: 2015-04-22, Last modification date: 2024-05-15) |
| Primary citation | Carneiro, M.G.,Koharudin, L.M.,Ban, D.,Sabo, T.M.,Trigo-Mourino, P.,Mazur, A.,Griesinger, C.,Gronenborn, A.M.,Lee, D. Sampling of Glycan-Bound Conformers by the Anti-HIV Lectin Oscillatoria agardhii agglutinin in the Absence of Sugar. Angew.Chem.Int.Ed.Engl., 54:6462-6465, 2015 Cited by PubMed 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. PubMed: 25873445DOI: 10.1002/anie.201500213 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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