A Unique Conformational Distortion Mechanism Drives Lipocalin 2 Binding to Bacterial Siderophores.

Huang, Xiaojing; Slavkovic, Sladjana; Song, Erfei; Botta, Amy; Mehrazma, Banafsheh; Lento, Cristina; Johnson, Philip E; Sweeney, Gary; Wilson, Derek J

Huang, Xiaojing; Slavkovic, Sladjana; Song, Erfei; Botta, Amy; Mehrazma, Banafsheh; Lento, Cristina; Johnson, Philip E; Sweeney, Gary; Wilson, Derek J.

ACS Chem Biol ; 15(1): 234-242, 2020 01 17.

Article in En | MEDLINE | ID: mdl-31613081

Subject(s)

Anti-Infective Agents/chemistry; Bacterial Proteins/chemistry; Deuterium/chemistry; Lipocalin-2/chemistry; Siderophores/chemistry; Anti-Infective Agents/metabolism; Bacterial Proteins/metabolism; Cell Line; Dose-Response Relationship, Drug; Drug Discovery; Enterobactin/chemistry; Humans; Hydroxybenzoates/chemistry; Immunity, Innate/drug effects; Iron/chemistry; Kinetics; Lipocalin-2/metabolism; Molecular Docking Simulation; Protein Binding; Protein Conformation; Reactive Oxygen Species/metabolism; Siderophores/metabolism; Staining and Labeling; Structure-Activity Relationship

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Siderophores / Deuterium / Lipocalin-2 / Anti-Infective Agents Limits: Humans Language: En Journal: ACS Chem Biol Year: 2020 Document type: Article

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