The Recognition Unit of FIBCD1 Organizes into a Noncovalently Linked Tetrameric Structure and Uses a Hydrophobic Funnel (S1) for Acetyl Group Recognition

• Published in: The Journal of biological chemistry Vol. 285; no. 2; pp. 1229 - 1238
• Main Authors: Thomsen, Theresa, Moeller, Jesper B., Schlosser, Anders, Sorensen, Grith L., Moestrup, Soren K., Palaniyar, Nades, Wallis, Russell, Mollenhauer, Jan, Holmskov, Uffe
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 08.01.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Substitution; Animals; Binding Sites - physiology; Carbohydrate/Complex; Cattle; Cell/Endocytosis; Chitin - chemistry; Chitin - genetics; Chitin - metabolism; Humans; Immunology/Innate Immunity; Methods/Site-directed Mutagenesis; Mutagenesis, Site-Directed; Mutation, Missense; Protein Binding - physiology; Protein Structure and Folding; Protein Structure, Quaternary - physiology; Protein Structure, Tertiary - physiology; Protein/Ligand Binding; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - genetics; Receptors, Cell Surface - metabolism; Receptors/Membrane; Structural Homology, Protein; Structure-Activity Relationship; Immunology/Innate Immunity; Carbohydrate/Complex; Protein/Ligand Binding; Receptors/Membrane; Cell/Endocytosis; Methods/Site-directed Mutagenesis

We have recently identified FIBCD1 (Fibrinogen Cdomain containing 1) as a type II transmembrane endocytic receptor located primarily in the intestinal brush border. The ectodomain of FIBCD1 comprises a coiled coil, a polycationic region, and a C-terminal FReD (fibrinogen-related domain) that assembl...