1OO2

Crystal structure of transthyretin from Sparus aurata

1OO2 の概要

• エントリーDOI: 10.2210/pdb1oo2/pdb
• 関連するPDBエントリー: 1F41 1FHN 1IE4 1qab 1RLB
• 分子名称: transthyretin, CADMIUM ION (3 entities in total)
• 機能のキーワード: transthyretin, retinol-binding protein, tetramer, transport protein
• 由来する生物種: Sparus aurata (gilthead seabream)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51538.12

構造登録者

Pasquato, N.,Ramazzina, I.,Folli, C.,Battistutta, R.,Berni, R.,Zanotti, G. (登録日: 2003-03-03, 公開日: 2004-01-20, 最終更新日: 2023-08-16)

主引用文献

Folli, C.,Pasquato, N.,Ramazzina, I.,Battistutta, R.,Zanotti, G.,Berni, R.
Distinctive binding and structural properties of piscine transthyretin.
Febs Lett., 555:279-284, 2003

PubMed Abstract: 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 A 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.

PubMed: 14644428
DOI: 10.1016/S0014-5793(03)01248-1

実験手法

X-RAY DIFFRACTION (1.56 Å)