Ficolins and FIBCD1: soluble and membrane bound pattern recognition molecules with acetyl group selectivity.
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.
Institute of Molecular Medicine, University of Southern Denmark, Denmark.
Theresa
T
Thomsen
Anders
A
Schlosser
Uffe
U
Holmskov
Grith L
GL
Sorensen
D000085:Acetates / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D051192:Receptors, Pattern Recognition / Q000235:genetics / Q000378:metabolism*; D012995:Solubility; D013379:Substrate Specificity; D000097604:Ficolins
D000085:Acetates; D037102:Lectins; D051192:Receptors, Pattern Recognition; D000097604:Ficolins