The conserved core domains of annexins A1, A2, A5, and B12 can be divided into two groups with different Ca2+-dependent membrane-binding properties.

@article{Patel2005TheCC,
  title={The conserved core domains of annexins A1, A2, A5, and B12 can be divided into two groups with different Ca2+-dependent membrane-binding properties.},
  author={Darshana R Patel and Jose Mario Isas and Alexey S. Ladokhin and Christine C. Jao and Yujin E Kim and Thorsten Kirsch and Ralf Langen and Harry T. Haigler},
  journal={Biochemistry},
  year={2005},
  volume={44 8},
  pages={2833-44}
}
The hallmark of the annexin super family of proteins is Ca(2+)-dependent binding to phospholipid bilayers, a property that resides in the conserved core domain of these proteins. Despite the structural similarity between the core domains, studies reported herein showed that annexins A1, A2, A5, and B12 could be divided into two groups with distinctively different Ca(2+)-dependent membrane-binding properties. The division correlates with the ability of the annexins to form Ca(2+)-dependent… CONTINUE READING