Correlation between conformation and antibody binding: NMR structure of cross‐reactive peptides from T. cruzi, human and L. braziliensis

Almeida F.C.L; Bisch P.M; Campos de Carvalho A.C; Soares M.R; Valente A.P

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Correlation between conformation and antibody binding: NMR structure of cross‐reactive peptides from T. cruzi, human and L. braziliensis

机译：构象与抗体结合之间的相关性：来自克鲁氏T，人和巴西乳杆菌的交叉反应肽的NMR结构

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>The structure of peptides corresponding to the C-terminal residues from Trypanosoma cruzi (R13), human (H13) and Leishmania braziliensis (A13) ribosomal proteins were determined using nuclear magnetic resonance. Although there is only one amino acid difference between them, the peptides present distinct structures in solution: R13 adopts a random coil conformation while H13 and A13 form a bend. Interaction of these peptides with polyclonal antibodies from chronic Chagas’ disease patients and a monoclonal antibody raised against T. cruzi ribosomal P2β protein was probed by transferred NOE. The results show that the flexibility of R13 is fundamental for the binding to the antibody.

机译：>使用以下方法确定了对应于 Trypanosoma cruzi （R13），人（H13）和 braishiliia braziliensis（em13）（A13）核糖体蛋白C末端残基的肽的结构核磁共振。尽管它们之间只有一个氨基酸差异，但是这些肽在溶液中呈现出不同的结构：R13采用无规卷曲构象，而H13和A13形成弯曲。这些肽与慢性恰加斯病患者的多克隆抗体以及针对 T的单克隆抗体相互作用。用转移的NOE方法检测了cruzi 核糖体P2β蛋白。结果表明，R13的柔韧性是与抗体结合的基础。 展开▼

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《FEBS Letters》 |2004年第3期|共页

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Almeida F.C.L; Bisch P.M; Campos de Carvalho A.C; Soares M.R; Valente A.P;
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中图分类分子生物学;

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Correlation between conformation and antibody binding: NMR structure of cross‐reactive peptides from T. cruzi, human and L. braziliensis

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