Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wright LM, Reynolds CD, Rizkallah PJ, Allen AK, Van Damme EJ, Donovan MJ, Peumans WJ. Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin. FEBS Lett. 2000 Feb 18;468(1):19-22. PMID:10683433
