Distinctive binding and structural properties of piscine transthyretin

FEBS Letters

Pasquato, Nicola²  Zanotti, Giuseppe²  Battistutta, Roberto²  Berni, Rodolfo¹  Ramazzina, Ileana¹  Folli, Claudia¹ 

[1] Department of Biochemistry and Molecular Biology, University of Parma, Parco Area delle Scienze 23/A, 43100 Parma, Italy;Department of Organic Chemistry, University of Padova, and Institute of Biomolecular Chemistry, Padova Section, Via Marzolo 1, 35131 Padua, Italy

关键词: Transthyretin;    Retinol binding protein;    Thyroid hormone;    Protein–protein interaction;    Crystal structure;    TTR;    transthyretin;    RBP;    retinol binding protein;    rmsd;    root mean square deviation;   

DOI  :  10.1016/S0014-5793(03)01248-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The thyroid hormone binding protein transthyretin (TTR) forms a macromolecular complex with the retinol-specific carrier retinol binding protein (RBP) in the blood of higher vertebrates. Piscine TTR is shown here to exhibit high binding affinity for L-thyroxine and negligible affinity for RBP. The 1.56 Å resolution X-ray structure of sea bream TTR, compared with that of human TTR, reveals a high degree of conservation of the thyroid hormone binding sites. In contrast, some amino acid differences in discrete regions of sea bream TTR appear to be responsible for the lack of protein–protein recognition, providing evidence for the crucial role played by a limited number of residues in the interaction between RBP and TTR. Overall, this study makes it possible to draw conclusions on evolutionary relationships for RBPs and TTRs of phylogenetically distant vertebrates.

【 授权许可】

Unknown