Cysteine 230 is essential for the structure and activity of the cytotoxic ligand TRAIL.

Fiche du document

Auteurs
Date

2000

Type de document
Périmètre
Langue
Identifiants
Source

Serveur académique Lausannois

Relations

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M909721199

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/10748154

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pissn/0021-9258

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_15C09F6E6B8D4

Collection

Serveur Académique Lausannois

Organisation

Université de Lausanne et CHUV

Licences

info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer

Mots-clés 0

Amino Acid Sequence; Apoptosis; Apoptosis Regulatory Proteins; Binding Sites; Cysteine/chemistry; Disulfides/chemistry; Humans; Hydrogen-Ion Concentration; Membrane Glycoproteins/chemistry; Membrane Glycoproteins/genetics; Molecular Sequence Data; Mutation; Protein Conformation; Receptors, Tumor Necrosis Factor/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Alignment; TNF-Related Apoptosis-Inducing Ligand; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha/chemistry; Tumor Necrosis Factor-alpha/genetics; Zinc/chemistry

Sujets proches En

Zinc systeinate Half-cysteine L-cysteine Cysteine hydrochloride

Citer ce document

J.L. Bodmer et al., « Cysteine 230 is essential for the structure and activity of the cytotoxic ligand TRAIL. », Serveur académique Lausannois, ID : 10.1074/jbc.M909721199

Métriques

Partage / Export

Résumé 0

Unlike other tumor necrosis factor family members, the cytotoxic ligand tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)/Apo-2L contains an unpaired cysteine residue (Cys(230)) in its receptor-binding domain. Here we show that the biological activity of both soluble recombinant TRAIL and cell-associated, full-length TRAIL is critically dependent on the presence of Cys(230). Mutation of Cys(230) to alanine or serine strongly affected its ability to kill target cells. Binding to its receptors was decreased by at least 200-fold, and the stability of its trimeric structure was reduced. In recombinant TRAIL, Cys(230) was found engaged either in interchain disulfide bridge formation, resulting in poorly active TRAIL, or in the chelation of one zinc atom per TRAIL trimer in the active, pro-apoptotic form of TRAIL.

document thumbnail

Par les mêmes auteurs

Sur les mêmes sujets

Exporter en