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

FEBS Letters

Soares, M.R¹  Almeida, F.C.L²  Valente, A.P²  Bisch, P.M¹  Campos de Carvalho, A.C¹ 

[1] Instituto de Biofı́sica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, 21941-590 Rio de Janeiro, RJ, Brazil;Centro Nacional de Ressonância Magnética Nuclear, Departamento de Bioquı́mica Médica – ICB/CCS, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Trompowiski s/n, CCS, Bloco E sala 10, 21941-590 Rio de Janeiro, RJ, Brazil

关键词: Ribosomal P protein;    Chagas’ disease;    Nuclear magnetic resonance;    Molecular recognition;   

DOI  :  10.1016/S0014-5793(04)00088-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown