Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.

@article{Randazzo2001StructuralII,
  title={Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.},
  author={A Randazzo and Christian Acklin and Beat W. Sch{\"a}fer and Claus Wilhelm Heizmann and Walter J Chazin},
  journal={Biochemical and biophysical research communications},
  year={2001},
  volume={288 2},
  pages={462-7}
}
The S100 subfamily of EF-hand proteins is distinguished by the binding of Zn(2+) in addition to Ca(2+). In an effort to understand the role of Zn(2+) in modulating the activity of S100 proteins, we have carried out heteronuclear NMR studies of Zn(2+)-bound S100A2 and obtained near complete resonance assignments. This analysis revealed an equilibrium between multiple isoforms due to cis-trans isomerism of proline residues in flexible regions of the protein. The secondary structure of S100A2 has… CONTINUE READING

From This Paper

Topics from this paper.