1ov3
From Proteopedia
(New page: 200px<br /> <applet load="1ov3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ov3, resolution 1.80Å" /> '''Structure of the p2...) |
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| - | [[Image:1ov3.gif|left|200px]]<br /> | + | [[Image:1ov3.gif|left|200px]]<br /><applet load="1ov3" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ov3" size=" | + | |
caption="1ov3, resolution 1.80Å" /> | caption="1ov3, resolution 1.80Å" /> | ||
'''Structure of the p22phox-p47phox complex'''<br /> | '''Structure of the p22phox-p47phox complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The multi-subunit NADPH oxidase complex plays a crucial role in host | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OV3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1OV3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OV3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lapouge, K.]] | [[Category: Lapouge, K.]] | ||
[[Category: Rittinger, K.]] | [[Category: Rittinger, K.]] | ||
| - | [[Category: Smerdon, S | + | [[Category: Smerdon, S J.]] |
[[Category: complex]] | [[Category: complex]] | ||
[[Category: nadph oxidase]] | [[Category: nadph oxidase]] | ||
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[[Category: p47phox]] | [[Category: p47phox]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:52 2008'' |
Revision as of 12:21, 21 February 2008
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Structure of the p22phox-p47phox complex
Contents |
Overview
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.
Disease
Known disease associated with this structure: Chronic granulomatous disease due to deficiency of NCF-1 OMIM:[608512]
About this Structure
1OV3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular basis of phosphorylation-induced activation of the NADPH oxidase., Groemping Y, Lapouge K, Smerdon SJ, Rittinger K, Cell. 2003 May 2;113(3):343-55. PMID:12732142
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