Structure of the extracellular domains of human andXenopusFn14: implications in the evolution of TWEAK and Fn14 interactions

Autor:	Pascal Schneider, Laure Willen, Eric S. Day, Dennis Krushinskie, Timothy S. Zheng, Mai Perroud, Hernan Cuervo, Kathy Strauch, Maria Pellegrini
Rok vydání:	2013
Předmět:	Models Molecular Protein Folding Molecular Sequence Data Xenopus Xenopus Proteins Biology 010402 general chemistry 01 natural sciences Biochemistry Protein Structure Secondary Receptors Tumor Necrosis Factor Xenopus laevis 03 medical and health sciences Protein structure Animals Humans Amino Acid Sequence Surface plasmon resonance Molecular Biology Peptide sequence Cytokine TWEAK 030304 developmental biology 0303 health sciences Cell Biology computer.file_format Ligand (biochemistry) Protein Data Bank biology.organism_classification Molecular biology Protein Structure Tertiary 0104 chemical sciences Cell biology evolution Fn14 NMR tumor necrosis factor TWEAK Mutagenesis TWEAK Receptor Tumor Necrosis Factors Protein folding Extracellular Space computer
Zdroj:	The FEBS journal FEBS Journal, vol. 280, no. 8, pp. 1818-1829
ISSN:	1742-464X
DOI:	10.1111/febs.12206
Popis:	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)
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5815066ef65850b703d4b976447dd80f https://doi.org/10.1111/febs.12206 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
Nepřihlášeným uživatelům se plný text nezobrazuje	K zobrazení výsledku je třeba se přihlásit.