2MSB

STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN COMPLEXED WITH AN OLIGOSACCHARIDE

Summary for 2MSB

• Entry DOI: 10.2210/pdb2msb/pdb
• Descriptor: MANNOSE-BINDING PROTEIN-A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: lectin
• Biological source: Rattus rattus (rodents)
• Total number of polymer chains: 2
• Total formula weight: 26810.82

Authors

Weis, W.I.,Drickamer, K.,Hendrickson, W.A. (deposition date: 1992-07-28, release date: 1993-10-31, Last modification date: 2024-11-13)

Primary citation

Weis, W.I.,Drickamer, K.,Hendrickson, W.A.
Structure of a C-type mannose-binding protein complexed with an oligosaccharide.
Nature, 360:127-134, 1992

PubMed Abstract: C-type (Ca(2+)-dependent) animal lectins such as mannose-binding proteins mediate many cell-surface carbohydrate-recognition events. The crystal structure at 1.7 A resolution of the carbohydrate-recognition domain of rat mannose-binding protein complexed with an oligomannose asparaginyl-oligosaccharide reveals that Ca2+ forms coordination bonds with the carbohydrate ligand. Carbohydrate specificity is determined by a network of coordination and hydrogen bonds that stabilizes the ternary complex of protein, Ca2+ and sugar. Two branches of the oligosaccharide crosslink neighbouring carbohydrate-recognition domains in the crystal, enabling multivalent binding to a single oligosaccharide chain to be visualized directly.

PubMed: 1436090
DOI: 10.1038/360127a0

Experimental method

X-RAY DIFFRACTION (1.7 Å)