Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin.
FEBS Lett
; 468(1): 19-22, 2000 Feb 18.
Article
en En
| MEDLINE
| ID: mdl-10683433
ABSTRACT
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.
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Banco de datos:
MEDLINE
Asunto principal:
Alfa-Fetoproteínas
/
Proteínas Portadoras
/
Liliaceae
/
Lectinas de Unión a Manosa
/
Lectinas
Idioma:
En
Revista:
FEBS Lett
Año:
2000
Tipo del documento:
Article
País de afiliación:
Reino Unido