{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T10:18:27Z","timestamp":1787480307943,"version":"build-2736575974"},"reference-count":31,"publisher":"Wiley","issue":"17","license":[{"start":{"date-parts":[[2006,7,31]],"date-time":"2006-07-31T00:00:00Z","timestamp":1154304000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2006,9]]},"abstract":"<jats:p>The relationship between the structure of the N\u2010terminal sequence of transthyretin (TTR) and the binding of thyroid hormone was studied. A recombinant human TTR and two derivatives of <jats:italic>Crocodylus porosus<\/jats:italic> TTRs, one with the N\u2010terminal sequence replaced by that of human TTR (human\/crocTTR), the other with the N\u2010terminal segment removed (truncated crocTTR), were synthesized in <jats:italic>Pichia pastoris<\/jats:italic>. Subunit mass, native molecular weight, tetramer formation, cross\u2010reactivity to TTR antibodies and binding to retinol\u2010binding protein of these recombinant TTRs were similar to TTRs found in nature. Analysis of the binding affinity to thyroid hormones of recombinant human TTR showed a dissociation constant (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>) for triiodothyronine (T3) of 53.26\u2003\u00b1\u20033.97\u2003n<jats:sc>m<\/jats:sc> and for thyroxine (T4) of 19.73\u2003\u00b1\u20030.13\u2003n<jats:sc>m<\/jats:sc>. These values are similar to those found for TTR purified from human serum, and gave a <jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub> T3\/T4 ratio of 2.70. The affinity for T4 of human\/crocTTR (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>\u2003=\u200322.75\u2003\u00b1\u20031.89\u2003n<jats:sc>m<\/jats:sc>) was higher than those of both human TTR and <jats:italic>C.\u2003porosus<\/jats:italic> TTR, but the affinity for T3 (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>\u2003=\u20035.40\u2003\u00b1\u20030.25\u2003n<jats:sc>m<\/jats:sc>) was similar to <jats:italic>C.\u2003porosus<\/jats:italic> TTR, giving a <jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub> T3\/T4 ratio of 0.24. A similar affinity for both T3 (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>\u2003=\u200357.78\u2003\u00b1\u20035.65\u2003n<jats:sc>m<\/jats:sc>) and T4 (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>\u2003=\u200359.72\u2003\u00b1\u20033.38\u2003n<jats:sc>m<\/jats:sc>), with a <jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub> T3\/T4 ratio of 0.97, was observed for truncated crocTTR. The obtained results strongly confirm the hypothesis that the unstructured N\u2010terminal region of TTR critically influences the specificity and affinity of thyroid hormone binding to TTR.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2006.05404.x","type":"journal-article","created":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T17:25:14Z","timestamp":1154453114000},"page":"4013-4023","source":"Crossref","is-referenced-by-count":31,"title":["Change in structure of the N\u2010terminal region of transthyretin produces change in affinity of transthyretin to T4 and 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