Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 Å resolution

Goretti Mallorquí-Fernández, Joan Pous, Rosa Peracaula, Joan Aymamí, Takashi Maeda, Hiroko Tada, Hidenori Yamada, Masaharu Seno, Rafael De Llorens, F. Xavier Gomis-Rüth, Miquel Coll

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59 Citations (Scopus)


Eosinophil cationic protein (ECP; RNase 3) is a human ribonuclease found only in eosinophil leukocytes that belongs to the RNase A superfamily. This enzyme is bactericidal, helminthotoxic and cytotoxic to mammalian cells and tissues. The protein has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data up to 1.75 Å resolution. The molecule displays the α + β folding topology typical for members of the ribonuclease A superfamily. The catalytic active site residues are conserved with respect to other ribonucleases of the superfamily but some differences appear at substrate recognition subsites, which may account, in part, for the low catalytic activity. Most strikingly, 19 surface-located arginine residues confer a strong basic character to the protein. The high concentration of positive charges and the particular orientation of the side-chains of these residues may also be related to the low activity of ECP as a ribonuclease and provides an explanation for its unique cytotoxic role through cell membrane disruption. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)1297-1307
Number of pages11
JournalJournal of Molecular Biology
Issue number5
Publication statusPublished - Jul 28 2000


  • Cytotoxicity
  • Eosinophil cationic protein (ECP)
  • RNase 3
  • X-ray crystal structure

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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