期刊
MOLECULAR IMMUNOLOGY
卷 48, 期 4, 页码 369-381出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2010.09.019
关键词
Ficolin; FIBCD1; Pattern recognition; Acetyl-group; Fibrinogen related domains
A network of molecules, which recognizes pathogens, work together to establish a quick and efficient immune response to infectious agents. Molecules containing a fibrinogen related domain in invertebrates and vertebrates have been implicated in immune responses against pathogens, and characterized as pattern recognition molecules. Ficolins are soluble oligomeric proteins composed of trimeric collagen-like regions linked to fibrinogen-related domains (FReDs) that have the ability to sense molecular patterns on both pathogens and apoptotic cell surfaces and activate the complement system. The ficolins have acetyl-binding properties, which have been localized to different binding sites in the FReD-region. A newly discovered tetrameric transmembrane protein, FIBCD1, likewise binds acetylated structures via the highly conserved FReD. This review presents current knowledge on acetyl binding FReD-containing molecules, and discusses structural resemblance but also diversity in recognition of acetylated ligands. (C) 2010 Elsevier Ltd. All rights reserved.
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