| Structural insights into the recognition properties of human ficolins. | |
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MedLine Citation:
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PMID: 20375619 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Virginie Garlatti; Lydie Martin; Monique Lacroix; Evelyne Gout; Gérard J Arlaud; Nicole M Thielens; Christine Gaboriaud |
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Publication Detail:
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Type: Journal Article; Review Date: 2009-08-06 |
Journal Detail:
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Title: Journal of innate immunity Volume: 2 ISSN: 1662-8128 ISO Abbreviation: J Innate Immun Publication Date: 2010 |
Date Detail:
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Created Date: 2010-04-08 Completed Date: 2010-08-05 Revised Date: 2011-11-04 |
Medline Journal Info:
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Nlm Unique ID: 101469471 Medline TA: J Innate Immun Country: Switzerland |
Other Details:
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Languages: eng Pagination: 17-23 Citation Subset: IM |
Copyright Information:
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(c) 2009 S. Karger AG, Basel. |
Affiliation:
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Institut de Biologie Structurale JP Ebel, Grenoble, France. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Carbohydrates
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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:
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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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