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Isothermal titration calorimetry was used to characterize the binding of calcium ion (Ca2+) and phospholipid to the peripheral membrane-binding protein annexin a5. The phospholipid was a binary mixture of a neutral and an acidic phospholipid, specifically phosphatidylcholine and phosphatidylserine in the form of large unilamellar vesicles. To stringently define the mode of binding, a global fit of...
The C2A domain is one of two calcium ion (Ca2+)- and membrane-binding domains within synaptotagmin I (Syt I), the identified Ca2+ sensor for regulated exocytosis of neurotransmitter. We propose that the mechanistic basis for C2A's response to Ca2+ and cellular function stems from marginal stability and ligand-induced redistributions of protein conformers. To test this hypothesis, we used a combination...