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1E3F

Structure of human transthyretin complexed with bromophenols: a new mode of binding

Summary for 1E3F
Entry DOI10.2210/pdb1e3f/pdb
Related1BM7 1BMZ 1BZ8 1BZD 1BZE 1E4H 1E5A 1ETA 1ETB 1QAB 1RLB 1THA 1THC 1TLM 1TSH 1TTA 1TTB 1TTC 1TTR 1TYR 2PAB 2ROX 2ROY
DescriptorTRANSTHYRETIN (2 entities in total)
Functional Keywordstransport(thyroxine), environmental pollutants, bromophenols
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationSecreted: P02766
Total number of polymer chains2
Total formula weight27554.72
Authors
Ghosh, M.,Meerts, I.A.T.M.,Cook, A.,Bergman, A.,Brouwer, A.,Johnson, L.N. (deposition date: 2000-06-14, release date: 2000-08-29, Last modification date: 2023-12-13)
Primary citationGhosh, M.,Meerts, I.A.T.M.,Cook, A.,Bergman, A.,Brouwer, A.,Johnson, L.N.
Structure of Human Transthyretin Complexed with Bromophenols : A New Mode of Binding
Acta Crystallogr.,Sect.D, 56:1085-, 2000
Cited by
PubMed Abstract: 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 thought to be a key ingredient for a strong binding to TTR, does not seem to play an important role in the binding of these compounds to TTR. In the TTR-PBP complex, it is primarily the halogens which interact with the TTR molecule and therefore must account for the strong affinity of binding. The interactions with the halogens are smaller in number in TTR-TBP and there is a decrease in affinity, even though the interaction with the hydroxyl group is stronger than that in the TTR-PBP complex.
PubMed: 10957627
DOI: 10.1107/S0907444900008568
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2024-11-06公开中

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