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

Article Details

Citation

Lapouge K, Smith SJ, Walker PA, Gamblin SJ, Smerdon SJ, Rittinger K

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

Mol Cell. 2000 Oct;6(4):899-907.

PubMed ID
11090627 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Ras-related C3 botulinum toxin substrate 1P63000Details
Neutrophil cytosol factor 2P19878Details