TWEAK binding to the Fn14 cysteine-rich domain depends on charged residues located in both the A1 and D2 modules.

ABSTRACT: TWEAK [TNF (tumour necrosis factor)-like weak inducer of apoptosis] is a member of the TNF superfamily of cytokines. TWEAK binds with high affinity to a single TNF receptor super-family member, Fn14 (fibroblast growth factor-inducible 14). This interaction can stimulate a variety of biological responses, depending on the cell type analysed. The murine Fn14 extracellular region is only 53 amino acids in length and primarily consists of a CRD (cysteine-rich domain) containing three disulphide bonds. In the present study, we investigated whether TWEAK binding to this CRD was dependent on selected evolutionarily conserved amino acid residues by using a site-specific mutagenesis approach and several different ligand-binding assays. Our results indicate that three residues within the predicted F

SUBMITTER: Brown SA 

PROVIDER: S-EPMC1513280 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature