The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide.

@article{Snook1998TheSA,
  title={The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide.},
  author={Colin Frank Snook and G. Andrew Woolley and Glaucius Oliva and Vasantha Pattabhi and Susan F. Wood and Tom L. Blundell and B. A. Wallace},
  journal={Structure},
  year={1998},
  volume={6 6},
  pages={
          783-92
        }
}
BACKGROUND Antiamoebin is a member of the peptaibol family of polypeptides and has a unique antibiotic activity: it acts as an antiamoebic agent, but does not effectively haemolyze erythrocytes even though it does exhibit membrane-modifying activity. RESULTS The structure of antiamoebin I has been determined by X-ray crystallography at 1.4 A resolution. The molecule forms a helical structure, which, as a result of the presence of a number of proline and hydroxyproline residues, has a deep… CONTINUE READING

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