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p47phox molecular activation for assembly of the neutrophil NADPH oxidase complex
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SYSNO ASEP 0354237 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title p47phox molecular activation for assembly of the neutrophil NADPH oxidase complex Author(s) Marcoux, J. (FR)
Man, Petr (MBU-M) RID, ORCID
Petit-Haertlein, I. (FR)
Vives, C. (FR)
Forest, E. (FR)
Fieschi, F. (FR)Source Title Journal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
Roč. 285, č. 37 (2010), s. 28980-28990Number of pages 11 s. Language eng - English Country US - United States Keywords SRC HOMOLOGY-3 DOMAINS ; PHOSPHORYLATION-INDUCED ACTIVATION ; TANDEM SH3 DOMAINS Subject RIV CE - Biochemistry CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000281594000063 DOI 10.1074/jbc.M110.139824 Annotation Paper describes mechanism of molecular activation of p47phox, one part of the NADPH oxidase complex. P47phox is a modular multidomain protein that is known to undergo process of activation via phosphorylation. Due to the modular nature and its size it is impossible to solve the structure of autoinhibited and activated form by NMR or crystallography. Therefore we used hydrogen/deuterium exchange coupled to mass spectrometry to describe the structural differences between the two forms. We show that the protein undergoes opening upon activation and described the key regions involved in the interaction in the auto-inhibited state Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2011
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