1HUP

HUMAN MANNOSE BINDING PROTEIN CARBOHYDRATE RECOGNITION DOMAIN TRIMERIZES THROUGH A TRIPLE ALPHA-HELICAL COILED-COIL

Summary for 1HUP

• Entry DOI: 10.2210/pdb1hup/pdb
• Descriptor: MANNOSE-BINDING PROTEIN, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: alpha-helical coiled-coil, c-type lectin
• Biological source: Homo sapiens (human)
• Cellular location: Secreted : P11226
• Total number of polymer chains: 1
• Total formula weight: 15889.02

Authors

Sheriff, S. (deposition date: 1994-09-21, release date: 1995-10-15, Last modification date: 2024-11-06)

Primary citation

Sheriff, S.,Chang, C.Y.,Ezekowitz, R.A.
Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil.
Nat.Struct.Biol., 1:789-794, 1994

PubMed Abstract: 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 alpha-helical coiled-coil. Each alpha-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.

PubMed: 7634089
DOI: 10.1038/nsb1194-789

Experimental method

X-RAY DIFFRACTION (2.5 Å)