JMB-HEADER RAS-JOURNALS EIMB Pleiades Publishing

RUS

             

ENG

YearIMPACT-FACTOR
2022  1,200
2021  1,540
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 44(2010) N 5 p. 832-835;
P.O. Tsvetkov1*, F. Devred2, A.A. Makarov1

Thermodynamics of Zinc Binding to Human S100A2

1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991
2INSERM UMR 911, CRO2, Aix-Marseille Université, Faculté de Pharmacie, Marseille, France

*tsvetkov@eimb.ru
Received - 2010-03-25; Accepted - 2010-04-28

Regulatory protein S100A2 is localized in the cell nucleus and takes part in the regulation of the cell cycle and cancerogenesis. It belongs to a large family of S100 proteins and can simultaneously bind calcium and zinc ions. Using a direct thermodynamical method of isothermal titration calorimetry we have determined that in the absence of calcium ions the S100A2 can bind three zinc ions per each monomer. Besides that, it was determined that the thermodynamics of zinc binding to different binding sites on the S100A2 are significantly different. Zinc binding to the first two sites on the S100A2 is enthalpically unfavorable and is driven only by entropic factors, while binding of the third zinc ion is enthalpically favorable. Analysis of the zinc ion adsorption isotherms shows that their binding occurs in a consecutive order.

S100A2, zinc ions, isothermal titration calorimetry



JMB-FOOTER RAS-JOURNALS