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Structural Insights into the Recognition Properties of Human FicolinsGarlatti V. · Martin L. · Lacroix M. · Gout E. · Arlaud G.J. · Thielens N.M. · Gaboriaud C.
Institut de Biologie Structurale JP Ebel, Grenoble, France Corresponding Author
Dr. Christine Gaboriaud
Institut de Biologie Structurale JP Ebel
41 rue Jules Horowitz
FR–38041 Grenoble Cedex 1 (France)
Tel. +33 4 3878 9599, Fax +33 4 3878 5122, E-Mail firstname.lastname@example.org
Innate immunity relies upon the ability of a variety of recognition molecules to sense pathogens through conserved molecular signatures that are often carbohydrates. Ficolins are oligomeric proteins assembled from collagen-like stalks and fibrinogen-like domains that have the ability to sense these molecular patterns on both pathogens and apoptotic cell surfaces. Three ficolins, termed L, H and M, have been identified in humans. They differ in their localization and concentration in extracellular fluids, their mode of secretion and their recognition properties. From a structural point of view, ficolins are assembled from basal trimeric subunits comprising a collagen-like triple helix and a globular domain composed of 3 fibrinogen-like domains. The globular domains are responsible for sensing danger signals whereas the collagen-like stalks provide a link with immune effectors. This review mainly focuses on the structure and recognition properties of the 3 human ficolins, as revealed by recent crystallographic analysis of their recognition domains. The ligand binding sites have been identified in the 3 ficolins and their recognition mechanisms have been characterized at the atomic level. In the case of M-ficolin, a structural transition at acidic pH disables the binding pocket, and thus likely participates in the functional cycle of this protein.
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