2d39

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spinqualitylabelsall models 2d39, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Trivalent Recognition Unit of Innate Immunity System; Crystal Structure of human M-ficolin Fibrinogen-like Domain

Overview

Ficolins are a kind of pathogen-recognition molecule in the innate immune, systems. To investigate the discrimination mechanism between self and, non-self by ficolins, we determined the crystal structure of the human, M-ficolin fibrinogen-like domain (FD1), which is the ligand-binding, domain, at 1.9A resolution. Although the FD1 monomer shares a common fold, with the fibrinogen gamma fragment and tachylectin-5A, the Asp-282-Cys-283, peptide bond, which is the predicted ligand-binding site on the C-terminal, P domain, is a normal trans bond, unlike the cases of the other two, proteins. The trimeric formation of FD1 results in the separation of the, three P domains, and the spatial arrangement of the three predicted, ligand-binding sites on the trimer is very similar to that of the trimeric, collectin, indicating that such an arrangement is generally required for, pathogen-recognition. The ligand binding study of FD1 in solution, indicated that the recombinant protein binds to N-acetyl-d-glucosamine and, the peptide Gly-Pro-Arg-Pro and suggested that the ligand-binding region, exhibits a conformational equilibrium involving cis-trans isomerization of, the Asp-282-Cys-283 peptide bond. The crystal structure and the ligand, binding study of FD1 provide an insight of the self- and non-self, discrimination mechanism by ficolins.

About this Structure

2D39 is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.

Reference

Trivalent recognition unit of innate immunity system: Crystal structure of trimeric human M-ficolin fibrinogen-like domain., Tanio M, Kondo S, Sugio S, Kohno T, J Biol Chem. 2007 Feb 9;282(6):3889-95. Epub 2006 Dec 4. PMID:17148457

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