The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly

The study shows in the absence of Ca(sub 2+) the N-terminal construct of HsCen2 revealed a compact core conformation including four ant parallel alpha-helices and a short ant parallel beta-sheet, to the apo structure of other calcium regulatory. The three dimensional model for the N-terminal domain of HsCen1 based on the high sequence conservation shows very close structural properties, where Ca(sub 2+) of the apo-N terminal of HsCen1 and HsCen2 revealed a weak affinity not dependent on calcium.