Primate cathelicidin orthologues display different structures and membrane interactions.

@article{Morgera2009PrimateCO,
  title={Primate cathelicidin orthologues display different structures and membrane interactions.},
  author={Francesca Morgera and Lisa Vaccari and Nikolinka Antcheva and Denis Scaini and Sabrina Pacor and Alessandro Tossi},
  journal={The Biochemical journal},
  year={2009},
  volume={417 3},
  pages={727-35}
}
The human cathelicidin LL-37 displays both direct antibacterial activities and the capacity to modulate host-cell activities. These depend on structural characteristics that are subject to positive selection for variation, as observed in a previous analysis of the CAMP gene (encoding LL-37) in primates. The altered balance between cationic and anionic residues in different primate orthologues affects intramolecular salt-bridging and influences the stability of the helical conformation and… CONTINUE READING
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