1hup
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1hup" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hup, resolution 2.5Å" /> '''HUMAN MANNOSE BINDIN...)
Next diff →
Revision as of 15:16, 12 November 2007
|
HUMAN MANNOSE BINDING PROTEIN CARBOHYDRATE RECOGNITION DOMAIN TRIMERIZES THROUGH A TRIPLE ALPHA-HELICAL COILED-COIL
Overview
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.
About this Structure
1HUP is a Single protein structure of sequence from Homo sapiens with CA and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil., Sheriff S, Chang CY, Ezekowitz RA, Nat Struct Biol. 1994 Nov;1(11):789-94. PMID:7634089
Page seeded by OCA on Mon Nov 12 17:22:54 2007
