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The X-ray crystal structure of tachylectin-2 in complex with N-acetylglucosamine (GlcNAc) is described. The structure reveals a new lectin fold and is the first example of a five-bladed β-propeller protein. The planar arrangement of five carbohydrate-binding sites is consistent with a role in binding the terminal GlcNAc moieties typical of certain Gram-positive bacteria.
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Beisel HG, Kawabata S, Iwanaga S, Huber R, Bode W Tachylectin 2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. EMBO J. 18:1999;2313-2322. The X-ray crystal structure of tachylectin-2 in complex with N-acetylglucosamine (GlcNAc) is described. The structure reveals a new lectin fold and is the first example of a five-bladed β-propeller protein. The planar arrangement of five carbohydrate-binding sites is consistent with a role in binding the terminal GlcNAc moieties typical of certain Gram-positive bacteria.
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The roles of various C-type lectins in the immune system are reviewed. Emphasis is placed on explaining how saccharide-binding specificity, in conjunction with the geometrical arrangement of carbohydrate-recognition domains, dictates function.
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