1dlp
From Proteopedia
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STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN
Overview
The three-dimensional structure of a 244-residue, multivalent, fetuin-binding lectin, SCAfet, isolated from bluebell (Scilla campanulata), bulbs, has been solved at 3.3 A resolution by molecular replacement using, the coordinates of the 119-residue, mannose-binding lectin, SCAman, also, from bluebell bulbs. Unlike most monocot mannose-binding lectins, such as, Galanthus nivalis agglutinin from snowdrop bulbs, which fold into a single, domain, SCAfet contains two domains with approximately 55% sequence, identity, joined by a linker peptide. Both domains are made up of a, 12-stranded beta-prism II fold, with three putative carbohydrate-binding, sites, one on each subdomain. SCAfet binds to the complex saccharides of, various animal glycoproteins but not to simple sugars.
About this Structure
1DLP is a Single protein structure of sequence from Hyacinthoides hispanica. Full crystallographic information is available from OCA.
Reference
Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin., Wright LM, Reynolds CD, Rizkallah PJ, Allen AK, Van Damme EJ, Donovan MJ, Peumans WJ, FEBS Lett. 2000 Feb 18;468(1):19-22. PMID:10683433
Page seeded by OCA on Sun Nov 25 03:17:39 2007
