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High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine

2004Journal article Open access
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dc.contributor.authorEneqvist, Therese
dc.contributor.authorLundberg, Erik
dc.contributor.authorKarlsson, Anders
dc.contributor.authorHuang, Shenghua
dc.contributor.authorSantos, Cecilia
dc.contributor.authorPower, Deborah
dc.contributor.authorSauer-Eriksson, A. Elisabeth
dc.date.accessioned2014-10-22T13:06:17Z
dc.date.available2014-10-22T13:06:17Z
dc.date.issued2004
dc.description.abstractTransthyretin (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.por
dc.description.sponsorshipWe thank Anders Olofsson, Uwe H. Sauer, Andreas Ho¨rnberg, and Terese Bergfors for valuable discussions and critical reading of the manuscript.por
dc.identifier.citationTherese 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.por
dc.identifier.doihttp://dx.doi.org/ 10.1074/jbc.M313553200
dc.identifier.issn0021-9258
dc.identifier.otherAUT: DPO00386;
dc.identifier.urihttp://hdl.handle.net/10400.1/5404
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherAmerican Society for Biochemistry and Molecular Biologypor
dc.relation.publisherversionhttp://www.jbc.org/content/279/25/26411.longpor
dc.subjectTransthyretinpor
dc.titleHigh resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxinepor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage26416por
oaire.citation.issue25por
oaire.citation.startPage26411por
oaire.citation.titleThe Journal of Biological Chemistrypor
oaire.citation.volume279por
person.familyNameSantos
person.familyNamePower
person.givenNameCecilia
person.givenNameDeborah Mary
person.identifier.ciencia-id761A-7ED2-D68F
person.identifier.ciencia-id891A-8A44-3CAE
person.identifier.orcid0000-0001-6074-7825
person.identifier.orcid0000-0003-1366-0246
person.identifier.ridC-9032-2016
person.identifier.scopus-author-id7201458751
person.identifier.scopus-author-id7101806760
rcaap.rightsopenAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublication0f8d7c69-8b13-4668-a14b-2d4d6741a6dd
relation.isAuthorOfPublicationc68f5ffb-63f6-4c70-8957-29e464fb59c0
relation.isAuthorOfPublication.latestForDiscovery0f8d7c69-8b13-4668-a14b-2d4d6741a6dd

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