Document Detail


Structural insights into the recognition properties of human ficolins.
MedLine Citation:
PMID:  20375619     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Virginie Garlatti; Lydie Martin; Monique Lacroix; Evelyne Gout; Gérard J Arlaud; Nicole M Thielens; Christine Gaboriaud
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Publication Detail:
Type:  Journal Article; Review     Date:  2009-08-06
Journal Detail:
Title:  Journal of innate immunity     Volume:  2     ISSN:  1662-8128     ISO Abbreviation:  J Innate Immun     Publication Date:  2010  
Date Detail:
Created Date:  2010-04-08     Completed Date:  2010-08-05     Revised Date:  2011-11-04    
Medline Journal Info:
Nlm Unique ID:  101469471     Medline TA:  J Innate Immun     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  17-23     Citation Subset:  IM    
Copyright Information:
(c) 2009 S. Karger AG, Basel.
Affiliation:
Institut de Biologie Structurale JP Ebel, Grenoble, France.
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MeSH Terms
Descriptor/Qualifier:
Carbohydrates / immunology
Complement System Proteins / immunology
Humans
Immunity, Innate
Lectins / chemistry,  immunology*
N-Acetylneuraminic Acid / immunology
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Receptors, Pattern Recognition / immunology
Chemical
Reg. No./Substance:
0/Carbohydrates; 0/Lectins; 0/Receptors, Pattern Recognition; 0/ficolin; 131-48-6/N-Acetylneuraminic Acid; 9007-36-7/Complement System Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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