Title : The Plasticity of the Carbohydrate Recognition Domain Dictates the Exquisite Mechanism of Binding of Human Macrophage Galactose-Type Lectin.

Pub. Date : 2019 Nov 4

PMID : 31404475






4 Functional Relationships(s)
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1 The Plasticity of Carbohydrate Recognition Domain Dictates the Exquisite Mechanism of Binding of Human Macrophage Galactose-Type Lectin. Carbohydrates C-type lectin domain containing 10A Homo sapiens
2 NMR analysis of the MGL carbohydrate recognition domain (MGL-CRD, C181-H316) in the absence and presence of alpha-methyl GalNAc (alpha-MeGalNAc), a simple monosaccharide, shows that the MGL-CRD is highly dynamic and its structure is strongly altered upon ligand binding. Carbohydrates C-type lectin domain containing 10A Homo sapiens
3 NMR analysis of the MGL carbohydrate recognition domain (MGL-CRD, C181-H316) in the absence and presence of alpha-methyl GalNAc (alpha-MeGalNAc), a simple monosaccharide, shows that the MGL-CRD is highly dynamic and its structure is strongly altered upon ligand binding. Carbohydrates C-type lectin domain containing 10A Homo sapiens
4 NMR analysis of the MGL carbohydrate recognition domain (MGL-CRD, C181-H316) in the absence and presence of alpha-methyl GalNAc (alpha-MeGalNAc), a simple monosaccharide, shows that the MGL-CRD is highly dynamic and its structure is strongly altered upon ligand binding. Carbohydrates C-type lectin domain containing 10A Homo sapiens