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

M. Ghosh, I.A.T.M. Meerts, A. Cook, A. Bergman, A. Brouwer, L.N. Johnson

Research output: Contribution to JournalArticleAcademicpeer-review

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
Original languageEnglish
Pages (from-to)1085-1095
JournalActa Crystallographica Section D. Biological Crystallography
Volume56
DOIs
Publication statusPublished - 2000

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