1OO2

Crystal structure of transthyretin from Sparus aurata

Summary for 1OO2

• Entry DOI: 10.2210/pdb1oo2/pdb
• Related: 1F41 1FHN 1IE4 1RLB 1qab
• Descriptor: transthyretin, CADMIUM ION (3 entities in total)
• Functional Keywords: transthyretin, retinol-binding protein, tetramer, transport protein
• Biological source: Sparus aurata (gilthead seabream)
• Total number of polymer chains: 4
• Total formula weight: 51538.12

Authors

Pasquato, N.,Ramazzina, I.,Folli, C.,Battistutta, R.,Berni, R.,Zanotti, G. (deposition date: 2003-03-03, release date: 2004-01-20, Last modification date: 2023-08-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.56 Å)