PMID: 9434104Jan 20, 1998Paper

Ion-binding properties of recombinant S100beta and two derivatives with either an inactivated Ca2+ site II or a normalized Ca2+ site I

Biochimica Et Biophysica Acta
I DurusselJ Cox

Abstract

S100beta contains one unusual and one canonical Ca2+-binding motif. In this study, we measured Ca2+-binding and ensuing conformational changes of recombinant S100beta (rS100beta) and of two mutant forms in which either the canonical loop was inactivated (NoEF) or the unusual one replaced by a canonical one (Caloops). Caloops binds two Ca2+ per monomer with a 3-fold higher affinity than rS100beta; the affinity of NoEF was too low for accurate direct determination. All three proteins bind 3-4 Zn2+ per monomer. Tyrosine 17 fluorescence spectra showed a decrease of intensity upon binding of Ca2+ to the three proteins and an increase upon binding of Zn2+ to rS100beta and NoEF but not in Caloops. The fluorescence change as a function of the Ca2+ concentration yielded half-maximal changes ([Ca2+]0.5) at 1.7, 11.3 and 0.55 mM free Ca2+ for rS100beta NoEF and Caloops, respectively. Our data demonstrate that in S100beta alterations in one site can affect the Ca2+ binding properties of the other site.

References

Nov 10, 1992·Biochimica Et Biophysica Acta·S W BargerL J Van Eldik
Jan 1, 1989·Annual Review of Biochemistry·N C Strynadka, M N James
Dec 15, 1987·Brain Research·L J Van Eldik, D B Zimmer
Jan 1, 1995·Brain Research Bulletin·D B ZimmerW Song
Apr 1, 1996·Trends in Biochemical Sciences·B W Schäfer, C W Heizmann

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Citations

Nov 25, 2003·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Murielle Rabiller-Baudry, Bernard Chaufer
Sep 10, 2010·Cardiovascular Psychiatry and Neurology·Danna B Zimmer, David J Weber
May 10, 2016·PloS One·Małgorzata BajorAleksandra Wysłouch-Cieszyńska
Jul 21, 1998·The Journal of Biological Chemistry·C FranzC W Heizmann

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