Multimer formation and ligand recognition by the long pentraxin PTX3. Similarities and differences with the short pentraxins C-reactive protein and serum amyloid P component.

@article{Bottazzi1997MultimerFA,
  title={Multimer formation and ligand recognition by the long pentraxin PTX3. Similarities and differences with the short pentraxins C-reactive protein and serum amyloid P component.},
  author={Barbara Bottazzi and Val{\'e}rie Vouret-Craviari and Antonio Bastone and Luca de Gioia and Claudia Matteucci and Giuseppe Peri and Federico Spreafico and Mario Pausa and C D'Ettorre and Elisabetta Gianazza and Aldo Tagliabue and Mario Salmona and Francesco Saverio Tedesco and Martino Introna and Alberto Mantovani},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 52},
  pages={32817-23}
}
PTX3 is a prototypic long pentraxin consisting of a C-terminal 203-amino acid pentraxin-like domain coupled with an N-terminal 178-amino acid unrelated portion. The present study was designed to characterize the structure and ligand binding properties of human PTX3, in comparison with the classical pentraxins C-reactive protein and serum amyloid P component. Sequencing of Chinese hamster ovary cell-expressed PTX3 revealed that the mature secreted protein starts at residue 18 (Glu). Lectin… CONTINUE READING
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