Solution structure of a mammalian pcb-binding protein in complex with a pcb

Torleif Hard, Henry J. Barnes, Christina Larsson, Jan Ake Gustafsson, Johan Lund

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

Metabolites of polychlorinated biphenyls (PCBs) bind with high affinity to uteroglobin, a small homodimeric protein that also binds progesterone. We present the solution structure of the reduced form of rat uteroglobin in complex with a PCB methylsulphone, (MeSO2)2-TCB. The structure reveals the molecular basis for the accumulation of (MeSO2)2-TCB by uteroglobin. The structure also shows how ligand binding and release might be controlled by reduction/oxidation of two intermolecular disulphide bonds. Breakage of these bonds induces a local unfolding of the N- and C-termini and a separation of helices creating a channel into the binding site. These effects make the ligand binding cavity readily accessible to entry of the ligand.

Original languageEnglish (US)
Pages (from-to)983-989
Number of pages7
JournalNature Structural Biology
Volume2
Issue number11
DOIs
StatePublished - Nov 1995

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

Fingerprint Dive into the research topics of 'Solution structure of a mammalian pcb-binding protein in complex with a pcb'. Together they form a unique fingerprint.

Cite this