S100-annexin complexes--structural insights.

@article{RintalaDempsey2008S100annexinCI,
  title={S100-annexin complexes--structural insights.},
  author={Anne C. Rintala-Dempsey and Atoosa Rezvanpour and Gary S. Shaw},
  journal={The FEBS journal},
  year={2008},
  volume={275 20},
  pages={4956-66}
}
Annexins and S100 proteins represent two large, but distinct, calcium-binding protein families. Annexins are made up of a highly alpha-helical core domain that binds calcium ions, allowing them to interact with phospholipid membranes. Furthermore, some annexins, such as annexins A1 and A2, contain an N-terminal region that is expelled from the core domain on calcium binding. These events allow for the interaction of the annexin N-terminus with target proteins, such as S100. In addition, when an… CONTINUE READING

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Identification of a novel interaction between the Ca ( 2 + )binding protein S 100 A 11 and the Ca ( 2 + )and phospholipidbinding protein annexin A 6

  • N Chang, C Sutherland, +6 authors DP Wilson
  • Am J Physiol Cell Physiol
  • 2007

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