Structural highlights
Function
UTER_RAT Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of a mammalian PCB-binding protein in complex with a PCB.,Hard T, Barnes HJ, Larsson C, Gustafsson JA, Lund J Nat Struct Biol. 1995 Nov;2(11):983-9. PMID:7583672[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hard T, Barnes HJ, Larsson C, Gustafsson JA, Lund J. Solution structure of a mammalian PCB-binding protein in complex with a PCB. Nat Struct Biol. 1995 Nov;2(11):983-9. PMID:7583672
