Hydramacin-1, Structure and Antibacterial Activity of a Protein from the Basal Metazoan Hydra*

  title={Hydramacin-1, Structure and Antibacterial Activity of a Protein from the Basal Metazoan Hydra*},
  author={Sascha Jung and Andrew J. Dingley and René Augustin and Friederike Anton-Erxleben and Mareike Stanisak and Christoph Gelhaus and Thomas Gutsmann and Malte U. Hammer and Rainer Podschun and Alexandre Mjj Bonvin and Matthias Leippe and Thomas C. G. Bosch and Joachim Grötzinger},
  journal={Journal of Biological Chemistry},
  pages={1896 - 1905}
Hydramacin-1 is a novel antimicrobial protein recently discovered during investigations of the epithelial defense of the ancient metazoan Hydra. The amino acid sequence of hydramacin-1 shows no sequence homology to any known antimicrobial proteins. Determination of the solution structure revealed that hydramacin-1 possesses a disulfide bridge-stabilized αβ motif. This motif is the common scaffold of the knottin protein fold. The structurally closest relatives are the scorpion oxin-like… 

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