Structure of the TPR domain of p67phox in complex with Rac.GTP.

Détails

ID Serval
serval:BIB_EA5707BA527A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Structure of the TPR domain of p67phox in complex with Rac.GTP.
Périodique
Molecular Cell
Auteur⸱e⸱s
Lapouge K., Smith S.J., Walker P.A., Gamblin S.J., Smerdon S.J., Rittinger K.
ISSN
1097-2765 (Print)
ISSN-L
1097-2765
Statut éditorial
Publié
Date de publication
2000
Volume
6
Numéro
4
Pages
899-907
Langue
anglais
Résumé
p67phox is an essential part of the NADPH oxidase, a multiprotein enzyme complex that produces superoxide ions in response to microbial infection. Binding of the small GTPase Rac to p67phox is a key step in the assembly of the active enzyme complex. The structure of Rac.GTP bound to the N-terminal TPR (tetratricopeptide repeat) domain of p67phox reveals a novel mode of Rho family/effector interaction and explains the basis of GTPase specificity. Complex formation is largely mediated by an insertion between two TPR motifs, suggesting an unsuspected versatility of TPR domains in target recognition and in their more general role as scaffolds for the assembly of multiprotein complexes.
Mots-clé
Amino Acid Sequence, Binding Sites, Calorimetry, Guanosine Triphosphate/chemistry, Guanosine Triphosphate/metabolism, Humans, Models, Molecular, Molecular Sequence Data, NADPH Dehydrogenase/chemistry, NADPH Dehydrogenase/metabolism, Phosphoproteins/chemistry, Phosphoproteins/metabolism, Protein Structure, Secondary, Recombinant Proteins/chemistry, Recombinant Proteins/metabolism, Repetitive Sequences, Amino Acid, Sequence Alignment, Sequence Homology, Amino Acid, Thermodynamics, rac GTP-Binding Proteins/chemistry, rac GTP-Binding Proteins/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
28/11/2011 15:10
Dernière modification de la notice
20/08/2019 16:12
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