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Table of Contents
Vol. 2, No. 1, 2010
Issue release date: December 2009
Section title: Review
Free Access
J Innate Immun 2010;2:17–23

Structural Insights into the Recognition Properties of Human Ficolins

Garlatti V. · Martin L. · Lacroix M. · Gout E. · Arlaud G.J. · Thielens N.M. · Gaboriaud C.
Institut de Biologie Structurale JP Ebel, Grenoble, France
email 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 christine.gaboriaud@ibs.fr

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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.

© 2009 S. Karger AG, Basel

Article / Publication Details

First-Page Preview
Abstract of Review

Received: February 25, 2009
Accepted: May 26, 2009
Published online: August 06, 2009
Issue release date: December 2009

Number of Print Pages: 7
Number of Figures: 3
Number of Tables: 0

ISSN: 1662-811X (Print)
eISSN: 1662-8128 (Online)

For additional information: http://www.karger.com/JIN

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