PMID: 8594205Feb 23, 1996Paper

Structural basis for calcium binding by uteroglobins

Journal of Molecular Biology
H J BarnesM Gillner

Abstract

Uteroglobins, i.e. proteins with similar three-dimensional structure and ligand binding specificity to uteroglobin from rabbit uterus, have been found in rat, mouse and human lung. We have recently demonstrated the binding of calcium by human uteroglobin, and we have therefore tried to find potential binding sites for metals in the three-dimensional structure of uteroglobin by the use of two different computational procedures. A putative binding site for calcium in uteroglobin was identified by means of a hydrophobic contrast function. The spatial disposition of atoms that could ligand calcium in the putative calcium-binding site appears similar to that of the primary calcium-binding site of secretory phospholipase A2 enzymes, consisting of the carboxyl group of an aspartic acid residue and a loop providing three backbone carbonyl oxygens. From inspection of their primary sequences and three-dimensional structures, it became clear that this putative calcium-binding motif is conserved among uteroglobins from different species. The potential significance of the predicted site was investigated by site-directed point mutagenesis of human uteroglobin in which Asp46 was replaced by Asn or Lys. In both mutants, the ruthenium red and 4...Continue Reading

Citations

Feb 24, 2001·Annals of the New York Academy of Sciences·L Miele
Feb 24, 2001·Annals of the New York Academy of Sciences·G Singh, S L Katyal
Feb 24, 2001·Annals of the New York Academy of Sciences·J NiJ Klug
Sep 4, 1999·Clinical Chemistry and Laboratory Medicine : CCLM·T YamaguchiY Itoh
Jan 20, 2016·Expert Opinion on Therapeutic Targets·Maria E Laucho-ContrerasCaroline A Owen
May 2, 2002·Protein Engineering·K V BrindaS Vishveshwara
Jun 5, 2007·Journal of Molecular Biology·Liselotte KaiserAdnane Achour

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