Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.1/5404
Título: High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine
Autor: Eneqvist, Therese
Lundberg, Erik
Karlsson, Anders
Huang, Shenghua
Santos, Cecília R. A.
Power, Deborah
Sauer-Eriksson, A. Elisabeth
Palavras-chave: Transthyretin
Data: 2004
Editora: American Society for Biochemistry and Molecular Biology
Citação: Therese Eneqvist, Erik Lundberg, Anders Karlsson, Shenghua Huang, Cecília R. A. Santos, Deborah M. Power and A. Elisabeth Sauer-Eriksson, "American Society for Biochemistry and Molecular Biology!" in J. Biol. Chem. 2004, 279:26411-26416.
Resumo: Transthyretin (TTR) is an extracellular transport protein involved in the distribution of thyroid hormones and vitamin A. So far, TTR has only been found in vertebrates, of which piscine TTR displays the lowest sequence identity with human TTR (47%). Human and piscine TTR bind both thyroid hormones 3,5,3 -triiodo- L-thyronine (T3) and 3,5,3 ,5 -tetraiodo-L-thyronine (thyroxine, T4). Human TTR has higher affinity for T4 than T3, whereas the reverse holds for piscine TTR. X-ray structures of Sparus aurata (sea bream) TTR have been determined as the apo-protein at 1.75 Å resolution and bound to ligands T3 and T4, both at 1.9 Å resolution. The apo structure is similar to human TTR with structural changes only at -strand D. This strand forms an extended loop conformation similar to the one in chicken TTR. The piscine TTR T4 complex shows the T4-binding site to be similar but not identical to human TTR, whereas the TTR T3 complex shows the I3 halogen situated at the site normally occupied by the hydroxyl group of T4. The significantly wider entrance of the hormone- binding channel in sea bream TTR, in combination with its narrower cavity, provides a structural explanation for the different binding affinities of human and piscine TTR to T3 and T4.
Peer review: yes
URI: http://hdl.handle.net/10400.1/5404
DOI: http://dx.doi.org/ 10.1074/jbc.M313553200
Versão do Editor: http://www.jbc.org/content/279/25/26411.long
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