2MWH

NMR solution structure of ligand-free OAA

2MWH の概要

• エントリーDOI: 10.2210/pdb2mwh/pdb
• NMR情報: BMRB: 25324
• 分子名称: Anti-HIV lectin OAA (1 entity in total)
• 機能のキーワード: protein binding, sugar binding protein-antiviral protein complex, sugar binding protein/antiviral protein
• 由来する生物種: Planktothrix agardhii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13930.76

構造登録者

Lee, D.,Carneiro, M.G.,Koharudin, L.M.,Griesinger, C.,Gronenborn, A.M.,Ban, D.,Sabo, T.,Trigo-Mourino, P.,Mazur, A. (登録日: 2014-11-10, 公開日: 2015-04-22, 最終更新日: 2024-05-15)

主引用文献

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

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: 25873445
DOI: 10.1002/anie.201500213

実験手法

SOLUTION NMR