Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions.

Détails

Ressource 1Télécharger: 5_23438059_Postprint.pdf (1424.88 [Ko])
Etat: Serval
Version: Author's accepted manuscript
ID Serval
serval:BIB_EF3E28010192
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions.
Périodique
FEBS Journal
Auteur(s)
Pellegrini M., Willen L., Perroud M., Krushinskie D., Strauch K., Cuervo H., Day E.S., Schneider P., Zheng T.S.
ISSN
1742-4658 (Electronic)
ISSN-L
1742-464X
Statut éditorial
Publié
Date de publication
2013
Volume
280
Numéro
8
Pages
1818-1829
Langue
anglais
Résumé
TWEAK (TNF homologue with weak apoptosis-inducing activity) and Fn14 (fibroblast growth factor-inducible protein 14) are members of the tumor necrosis factor (TNF) ligand and receptor super-families. Having observed that Xenopus Fn14 cross-reacts with human TWEAK, despite its relatively low sequence homology to human Fn14, we examined the conservation in tertiary fold and binding interfaces between the two species. Our results, combining NMR solution structure determination, binding assays, extensive site-directed mutagenesis and molecular modeling, reveal that, in addition to the known and previously characterized β-hairpin motif, the helix-loop-helix motif makes an essential contribution to the receptor/ligand binding interface. We further discuss the insight provided by the structural analyses regarding how the cysteine-rich domains of the TNF receptor super-family may have evolved over time. DATABASE: Structural data are available in the Protein Data Bank/BioMagResBank databases under the accession codes 2KMZ, 2KN0 and 2KN1 and 17237, 17247 and 17252. STRUCTURED DIGITAL ABSTRACT: TWEAK binds to hFn14 by surface plasmon resonance (View interaction) xeFn14 binds to TWEAK by enzyme linked immunosorbent assay (View interaction) TWEAK binds to xeFn14 by surface plasmon resonance (View interaction) hFn14 binds to TWEAK by enzyme linked immunosorbent assay (View interaction).
Mots-clé
evolution, Fn14, NMR, tumor necrosis factor, TWEAK
Pubmed
Web of science
Open Access
Oui
Création de la notice
16/05/2013 8:13
Dernière modification de la notice
09/05/2019 3:12
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