Molecular basis for TANK recognition by TRAF1 revealed by the crystal structure of TRAF1/TANK complex.
FEBS Lett
; 591(5): 810-821, 2017 03.
Article
de En
| MEDLINE
| ID: mdl-28155233
ABSTRACT
Tumor necrosis factor receptor-associated factor 1 (TRAF1) is a multifunctional adaptor protein involved in important processes of cellular signaling, including innate immunity and apoptosis. TRAF family member-associated NF-kappaB activator (TANK) has been identified as a competitive intracellular inhibitor of TRAF2 function. Although TRAF recognition by various receptors has been studied extensively in the field of TRAF-mediated biology, molecular and functional details of TANK recognition and interaction with TRAF1 have not been studied. In this study, we report the crystal structure of the TRAF1/TANK peptide complex. Quantitative interaction experiments showed that TANK peptide interacts with both TRAF1 and TRAF2 with similar affinity in a micromolar range. Our structural study also reveals that TANK binds TRAF1 using a minor minimal consensus motif for TRAF binding, Px(Q/E)xT. DATABASE Coordinate and structural factor were deposited in the Protein Data Bank under PDB ID code 5H10.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Protéines adaptatrices de la transduction du signal
/
Facteur-1 associé aux récepteurs de TNF
/
Facteur-2 associé aux récepteurs de TNF
Type d'étude:
Prognostic_studies
Limites:
Humans
Langue:
En
Journal:
FEBS Lett
Année:
2017
Type de document:
Article
Pays d'affiliation:
Corée du Sud