Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
Détails
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Etat: Public
Version: de l'auteur⸱e
Etat: Public
Version: de l'auteur⸱e
ID Serval
serval:BIB_564FB3633D0E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
Périodique
Cell
ISSN
0092-8674 (Print)
Statut éditorial
Publié
Date de publication
02/2007
Peer-reviewed
Oui
Volume
128
Numéro
3
Pages
533-46
Langue
anglais
Notes
Journal Article --- Old month value: Feb 9
Résumé
Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry.
Mots-clé
Amino Acid Sequence
CRADD Signaling Adaptor Protein/*chemistry/genetics/*metabolism
Caspase 2/metabolism
Crystallography, X-Ray
Death Domain Receptor Signaling Adaptor
Proteins/*chemistry/genetics/*metabolism
Models, Molecular
Molecular Sequence Data
Multiprotein Complexes/*metabolism
Mutagenesis, Site-Directed
Protein Conformation
Protein Structure, Tertiary
Recombinant Proteins/chemistry/genetics/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:19
Dernière modification de la notice
20/08/2019 15:10