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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
37
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pubmed:dateCreated |
2010-9-6
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pubmed:abstractText |
The p47(phox) cytosolic factor from neutrophilic NADPH oxidase has always been resistant to crystallogenesis trials due to its modular organization leading to relative flexibility. Hydrogen/deuterium exchange coupled to mass spectrometry was used to obtain structural information on the conformational mechanism that underlies p47(phox) activation. We confirmed a relative opening of the protein with exposure of the SH3 Src loops that are known to bind p22(phox) upon activation. A new surface was shown to be unmasked after activation, representing a potential autoinhibitory surface that may block the interaction of the PX domain with the membrane in the resting state. Within this surface, we identified 2 residues involved in the interaction with the PX domain. The double mutant R162A/D166A showed a higher affinity for specific phospholipids but none for the C-terminal part of p22(phox), reflecting an intermediate conformation between the autoinhibited and activated forms.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20592030-10559253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20592030-10788501,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20592030-9879360
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1083-351X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
10
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28980-90
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pubmed:dateRevised |
2011-9-13
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pubmed:meshHeading |
pubmed-meshheading:20592030-Amino Acid Substitution,
pubmed-meshheading:20592030-Animals,
pubmed-meshheading:20592030-Enzyme Activation,
pubmed-meshheading:20592030-Humans,
pubmed-meshheading:20592030-Mutation, Missense,
pubmed-meshheading:20592030-NADPH Oxidase,
pubmed-meshheading:20592030-Neutrophils,
pubmed-meshheading:20592030-Protein Structure, Secondary,
pubmed-meshheading:20592030-src Homology Domains
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pubmed:year |
2010
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pubmed:articleTitle |
p47phox molecular activation for assembly of the neutrophil NADPH oxidase complex.
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pubmed:affiliation |
Laboratoire des Protéines Membranaires, Institut de Biologie Structurale (IBS), 41 rue Jules Horowitz, Grenoble, F-38027, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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