[PDF][PDF] Structure of the TPR Domain of p67phox in Complex with Rac· GTP
K Lapouge, SJM Smith, PA Walker, SJ Gamblin… - Molecular cell, 2000 - cell.com
K Lapouge, SJM Smith, PA Walker, SJ Gamblin, SJ Smerdon, K Rittinger
Molecular cell, 2000•cell.comAbstract p67 phox 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 p67 phox is a key step in the assembly of the active enzyme complex.
The structure of Rac· GTP bound to the N-terminal TPR (tetratrico-peptide repeat) domain of
p67 phox 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 …
complex that produces superoxide ions in response to microbial infection. Binding of the
small GTPase Rac to p67 phox is a key step in the assembly of the active enzyme complex.
The structure of Rac· GTP bound to the N-terminal TPR (tetratrico-peptide repeat) domain of
p67 phox 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 …
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 (tetratrico-peptide 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.
cell.com