The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption.

@article{Zhang2010TheMS,
  title={The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption.},
  author={Yuan Zhang and Wuyuan Lu and Mei Hong},
  journal={Biochemistry},
  year={2010},
  volume={49 45},
  pages={9770-82}
}
Defensins are cationic and disulfide-bonded host defense proteins of many animals that target microbial cell membranes. Elucidating the three-dimensional structure, dynamics, and topology of these proteins in phospholipid bilayers is important for understanding their mechanisms of action. Using solid-state nuclear magnetic resonance spectroscopy, we have now determined the conformation, dynamics, oligomeric state, and topology of a human α-defensin, HNP-1, in DMPC/DMPG bilayers. Two-dimensional… CONTINUE READING