Human ficolin-2 recognition versatility extended: an update on the binding of ficolin-2 to sulfated/phosphated carbohydrates.

Abstract : Ficolin-2 has been reported to bind to DNA and heparin, but the mechanism involved has not been thoroughly investigated. X-ray studies of the ficolin-2 fibrinogen-like domain in complex with several new ligands now show that sulfate and phosphate groups are prone to bind to the S3 binding site of the protein. Composed of Arg132, Asp133, Thr136 and Lys221, the S3 site was previously shown to mainly bind N-acetyl groups. Furthermore, DNA and heparin compete for binding to ficolin-2. Mutagenesis studies reveal that Arg132, and to a lesser extent Asp133, are important for this binding property. The versatility of the S3 site in binding N-acetyl, sulfate and phosphate groups is discussed through comparisons with homologous fibrinogen-like recognition proteins.
Type de document :
Article dans une revue
FEBS Letters, Wiley, 2014, 588 (24), pp.4694-700
Liste complète des métadonnées

http://hal.univ-grenoble-alpes.fr/hal-01119750
Contributeur : Frank Thomas <>
Soumis le : mardi 24 février 2015 - 08:14:40
Dernière modification le : vendredi 22 juin 2018 - 09:32:29

Identifiants

  • HAL Id : hal-01119750, version 1
  • PUBMED : 25447524

Citation

Emmanuelle Laffly, Monique Lacroix, Lydie Martin, Emilie Vassal-Stermann, Nicole Thielens, et al.. Human ficolin-2 recognition versatility extended: an update on the binding of ficolin-2 to sulfated/phosphated carbohydrates.. FEBS Letters, Wiley, 2014, 588 (24), pp.4694-700. 〈hal-01119750〉

Partager

Métriques

Consultations de la notice

406