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The crystal structure of human CD81 large extracellular domain is reported here at 1.6 resolution. Each subunit within the homodimeric protein displays a mushroom-like structure, composed of five -helices arranged in stalk and head subdomains.
Their basic structures include an N-terminal triple-helical collagen region and a homotrimeric ligand-recognition domain, called a C-type lectin or carbohydrate recognition domain (CRD). SP-D levels in surfactant lining of the alveolar epithelia are significantly less (10-fold) than SP-A.
CD81 interacts with a high stoichiometry with its partner proteins EWI-2, EWI-2wint, and EWI-F. These latter proteins modify the functions of CD81 and can thereby potentially inhibit infection or modulate cell migration.
The structure of the CD19-CD81 complex is elongated, with the Fab-bound CD19 ectodomain resting directly on top of the CD81 ectodomain and the transmembrane helices arranged in a five-helix bundle (Fig. 1AOpens in image viewer).
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