tailieunhanh - Báo cáo khoa học: Change in structure of the N-terminal region of transthyretin produces change in affinity of transthyretin to T4 and T3

The relationship between the structure of the N-terminal sequence of trans-thyretin (TTR) and the binding of thyroid hormone was studied. A recom-binant human TTR and two derivatives of Crocodylus porosusTTRs, one with the N-terminal sequence replaced by that of human TTR (human⁄crocTTR), the other with the N-terminal segment removed (trun-cated crocTTR), were synthesized inPichia pastoris. | ỊFEBS Journal Change in structure of the N-terminal region of transthyretin produces change in affinity of transthyretin to T4 and T3 Porntip Prapunpoj1 Ladda Leelawatwatana1 Gerhard Schreiber2 and Samantha J. Richardson2 3 1 Department of Biochemistry Faculty of Science Prince of Songkla University Hat-Yai Songkhla Thailand 2 Department of Biochemistry and Molecular Biology Bio21 Molecular Science and Biotechnology Institute The University of Melbourne Parkville Victoria Australia 3 UMR CNRS 5166 Evolution des Regulations Endocriniennes Museum Nationald Histoire Naturelle Paris France Keywords N-terminalsequence protein evolution recombinant transthyretin thyroid hormone-binding plasma proteins thyroid hormone Correspondence P. Prapunpoj Department of Biochemistry Faculty of Science Prince of Songkla University Hat-Yai Songkhla 90112 Thailand Fax 66 74 446656 Tel 66 74 288275 E-mail Received 4 May 2006 revised 14 June 2006 accepted 3 July 2006 doi The relationship between the structure of the N-terminal sequence of transthyretin TTR and the binding of thyroid hormone was studied. A recombinant human TTR and two derivatives of Crocodylus porosus TTRs one with the N-terminal sequence replaced by that of human TTR human crocTTR the other with the N-terminal segment removed truncated crocTTR were synthesized in Pichia pastoris. Subunit mass native molecular weight tetramer formation cross-reactivity to TTR antibodies and binding to retinol-binding 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 Kd for triiodothyronine T3 of nM and for thyroxine T4 of nM. These values are similar to those found for TTR purified from human serum and gave a Kd T3 T4 ratio of . The affinity for T4 of human crocTTR Kd nM was higher than those of both human TTR and C. .

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