1e5a: Difference between revisions
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Revision as of 16:01, 30 October 2007
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STRUCTURE OF HUMAN TRANSTHYRETIN COMPLEXED WITH BROMOPHENOLS: A NEW MODE OF BINDING
OverviewOverview
The binding of two organohalogen substances, pentabromophenol (PBP) and, 2,4,6-tribromophenol (TBP), to human transthyretin (TTR), a thyroid, hormone transport protein, has been studied by in vitro competitive, binding assays and by X-ray crystallography. Both compounds bind to TTR, with high affinity, in competition with the natural ligand thyroxine, (T(4)). The crystal structures of the TTR-PBP and TTR-TBP complexes show, some unusual binding patterns for the ligands. They bind exclusively in, the 'reversed' mode, with their hydroxyl group pointing towards the mouth, of the binding channel and in planes approximately perpendicular to that, adopted by the T(4) phenolic ring in a TTR-T(4) complex, a feature not, observed before. The hydroxyl group in the ligands, which was previously, ... [(full description)]
About this StructureAbout this Structure
1E5A is a [Single protein] structure of sequence from [Homo sapiens] with TBP as [ligand]. Structure known Active Sites: 1 and 2. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of human transthyretin complexed with bromophenols: a new mode of binding., Ghosh M, Meerts IA, Cook A, Bergman A, Brouwer A, Johnson LN, Acta Crystallogr D Biol Crystallogr. 2000 Sep;56(Pt 9):1085-95. PMID:10957627
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