Structural and functional characterization of recombinant mouse annexin A11: influence of calcium binding.

@article{Lecona2003StructuralAF,
  title={Structural and functional characterization of recombinant mouse annexin A11: influence of calcium binding.},
  author={Emilio Lecona and Javier Turnay and Nieves Olmo and Ana I Guzm{\'a}n-Aranguez and Reginald O Morgan and M Z Fernandez and Ma Antonia Lizarbe},
  journal={The Biochemical journal},
  year={2003},
  volume={373 Pt 2},
  pages={437-49}
}
Annexin A11 is one of the 12 vertebrate subfamilies in the annexin superfamily of calcium/phospholipid-binding proteins, distinguishable by long, non-homologous N-termini rich in proline, glycine and tyrosine residues. As there is negligible structural information concerning this annexin subfamily apart from primary sequence data, we have cloned, expressed and purified recombinant mouse annexin A11 to investigate its structural and functional properties. CD spectroscopy reveals two main… CONTINUE READING

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