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

Details

Serval ID
serval:BIB_EA5707BA527A
Type
Article: article from journal or magazin.
Collection
Publications
Title
Structure of the TPR domain of p67phox in complex with Rac.GTP.
Journal
Molecular Cell
Author(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
Publication state
Published
Issued date
2000
Volume
6
Number
4
Pages
899-907
Language
english
Abstract
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.
Keywords
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
Yes
Create date
28/11/2011 15:10
Last modification date
20/08/2019 16:12
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