1oo2
From Proteopedia
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Crystal structure of transthyretin from Sparus aurata
Overview
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.
About this Structure
1OO2 is a Single protein structure of sequence from Sparus aurata with as ligand. Full crystallographic information is available from OCA.
Reference
Distinctive binding and structural properties of piscine transthyretin., Folli C, Pasquato N, Ramazzina I, Battistutta R, Zanotti G, Berni R, FEBS Lett. 2003 Dec 4;555(2):279-84. PMID:14644428
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