Structural Characterization of the Ceruloplasmin: Lactoferrin Complex in Solution

Annalaura Sabatucci, Patrice Vachette, Vadim B. Vasilyev, Mariano Beltramini, Alexey Sokolov, Maria Pulina, Benedetto Salvato, Clotilde B. Angelucci, Mauro Maccarrone, Ivo Cozzani, Enrico Dainese

Research output: Contribution to journalArticlepeer-review


Ceruloplasmin is a copper protein found in vertebrate plasma, which belongs to the family of multicopper oxidases. Like transferrin of the blood plasma, lactoferrin, the iron-containing protein of human milk, saliva, tears, seminal plasma and of neutrophilic leukocytes tightly binds two ferric ions. Human lactoferrin and ceruloplasmin have been previously shown to interact both in vivo and in vitro forming a complex. Here we describe a study of the conformation of the human lactoferrin/ceruloplasmin complex in solution using small angle X-ray scattering. Our ab initio structural analysis shows that the complex has a 1:1 stoichiometry and suggests that complex formation occurs without major conformational rearrangements of either protein. Rigid-body modeling of the mutual arrangement of proteins in the complex essentially yields two families of solutions. Final discrimination is possible when integrating in the modeling process extra information translating into structural constraints on the interaction between the two partners.

Original languageEnglish
Pages (from-to)1038-1046
Number of pages9
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - Aug 24 2007


  • complex
  • conformation in solution
  • human ceruloplasmin
  • human lactoferrin
  • SAXS

ASJC Scopus subject areas

  • Virology


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