English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Molecular basis of phosphorylation-induced activation of the NADPH oxidase

Groemping, Y., Lapouge, K., Smerdon, S. J., & Rittinger, K. (2003). Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell, 113(3), 343-355. doi:10.1016/S0092-8674(03)00314-3.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0000-3CAE-A Version Permalink: http://hdl.handle.net/21.11116/0000-0000-3CAF-9
Genre: Journal Article

Files

show Files
hide Files
:
Cell_113_2003_343.pdf (Any fulltext), 681KB
 
File Permalink:
-
Name:
Cell_113_2003_343.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, Heidelberg; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Groemping, Yvonne1, Author              
Lapouge, Karin, Author
Smerdon, Stephen J., Author
Rittinger, Katrin2, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: The multi-subunit NADPH oxidase complex plays a crucial role in host defense against microbial infection through the production of reactive oxygen species. Activation of the NADPH oxidase requires the targeting of a cytoplasmic p40-p47-p67(phox) complex to the membrane bound heterodimeric p22-gp91(phox) flavocytochrome. This interaction is prevented in the resting state due to an auto-inhibited conformation of p47(phox). The X-ray structure of the auto-inhibited form of p47(phox) reveals that tandem SH3 domains function together to maintain the cytoplasmic complex in an inactive form. Further structural and biochemical data show that phosphorylation of p47(phox) activates a molecular switch that relieves the inhibitory intramolecular interaction. This permits p47(phox) to interact with the cytoplasmic tail of p22(phox) and initiate formation of the active, membrane bound enzyme complex.

Details

show
hide
Language(s): eng - English
 Dates: 2003-03-052002-10-232003-03-312003-04-152003-05-02
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Cell
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 113 (3) Sequence Number: - Start / End Page: 343 - 355 Identifier: ISSN: 0092-8674
CoNE: /journals/resource/954925463183