EN
Porcine liver annexin VI (AnxVI) has recently been described to bind in vitro ATP. The binding of nucleotide to protein is accompanied by modulation of AnxVI function, such as its' interaction with F-actin and membranes. In the present report, we show that ATP modulates AnxVI-driven aggregation of phosphatidylserine (PS) liposomes. In addition, we provide evidence using circular dichroism (CD) that the interaction of AnxVI with ATP evokes changes in secondary structure of the protein. The functional implications of these changes are also discussed.