TY - JOUR
T1 - Structural Characterization of the Ceruloplasmin
T2 - Lactoferrin Complex in Solution
AU - Sabatucci, Annalaura
AU - Vachette, Patrice
AU - Vasilyev, Vadim B.
AU - Beltramini, Mariano
AU - Sokolov, Alexey
AU - Pulina, Maria
AU - Salvato, Benedetto
AU - Angelucci, Clotilde B.
AU - Maccarrone, Mauro
AU - Cozzani, Ivo
AU - Dainese, Enrico
PY - 2007/8/24
Y1 - 2007/8/24
N2 - 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.
AB - 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.
KW - complex
KW - conformation in solution
KW - human ceruloplasmin
KW - human lactoferrin
KW - SAXS
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U2 - 10.1016/j.jmb.2007.05.089
DO - 10.1016/j.jmb.2007.05.089
M3 - Article
C2 - 17597152
AN - SCOPUS:34547104636
VL - 371
SP - 1038
EP - 1046
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -