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nature portfolio permissions reprints privacy policy triple α-helical coiled-coil α-helical coiled-coil stalks advertising human mannose-binding protein social media nature genet mannose-binding protein multimerize nature 343 nature 360 nature 367 nature 371 nature 289 nature carbohydrate-recognition domains linked protein data bank stranded α-helical bundle related c-type lectins mannose-binding proteins isolated computer-based archival file hematology/oncology harvard department extracorporeal blood-cleansing device amino-terminal region rich mannose-rich salmonella montevideo collagenous c-type lectins calcium-dependent lectin domain collagen triple-helix formation carbohydrate recognition domain carbohydrate-recognition domain preliminary x-ray analysis mannose-binding protein e-selectin/ligand interaction springerlink instant access generalized molecular replacement mannan-binding protein permissions personal data mannose-rich isolate data protection human immunodeficiency virus α-helix interacts x-ray crystallography stranded coiled coils privacy proenzyme c1r2c1s2 complex yale university press basic recognition unit protein structure stabilization

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         headline:Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil
         description:Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a ‘neck’, and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the ‘neck’ and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The ‘neck’ forms a triple α-helical coiled-coil. Each α-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms.
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