2dyb
From Proteopedia
(New page: 200px<br /> <applet load="2dyb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dyb, resolution 3.15Å" /> '''The crystal structu...) |
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| - | [[Image:2dyb.gif|left|200px]]<br /> | + | [[Image:2dyb.gif|left|200px]]<br /><applet load="2dyb" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2dyb" size=" | + | |
caption="2dyb, resolution 3.15Å" /> | caption="2dyb, resolution 3.15Å" /> | ||
'''The crystal structure of human p40(phox)'''<br /> | '''The crystal structure of human p40(phox)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The superoxide-producing phagocyte NADPH oxidase is activated during | + | The superoxide-producing phagocyte NADPH oxidase is activated during phagocytosis to destroy ingested microbes. The adaptor protein p40phox associates via the PB1 domain with the essential oxidase activator p67phox, and is considered to function by recruiting p67phox to phagosomes; in this process, the PX domain of p40phox binds to phosphatidylinositol 3-phosphate [PtdIns(3)P], a lipid abundant in the phagosomal membrane. Here we show that the PtdIns(3)P-binding activity of p40phox is normally inhibited by the PB1 domain both in vivo and in vitro. The crystal structure of the full-length p40phox reveals that the inhibition is mediated via intramolecular interaction between the PB1 and PX domains. The interface of the p40phox PB1 domain for the PX domain localizes on the opposite side of that for the p67phox PB1 domain, and thus the PB1-mediated PX regulation occurs without preventing the PB1-PB1 association with p67phox. |
==About this Structure== | ==About this Structure== | ||
| - | 2DYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2DYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2DYB OCA]. |
==Reference== | ==Reference== | ||
| - | Full-length | + | Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding., Honbou K, Minakami R, Yuzawa S, Takeya R, Suzuki NN, Kamakura S, Sumimoto H, Inagaki F, EMBO J. 2007 Feb 21;26(4):1176-86. Epub 2007 Feb 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17290225 17290225] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: p40(phox)]] | [[Category: p40(phox)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:04:01 2008'' |
Revision as of 15:04, 21 February 2008
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The crystal structure of human p40(phox)
Overview
The superoxide-producing phagocyte NADPH oxidase is activated during phagocytosis to destroy ingested microbes. The adaptor protein p40phox associates via the PB1 domain with the essential oxidase activator p67phox, and is considered to function by recruiting p67phox to phagosomes; in this process, the PX domain of p40phox binds to phosphatidylinositol 3-phosphate [PtdIns(3)P], a lipid abundant in the phagosomal membrane. Here we show that the PtdIns(3)P-binding activity of p40phox is normally inhibited by the PB1 domain both in vivo and in vitro. The crystal structure of the full-length p40phox reveals that the inhibition is mediated via intramolecular interaction between the PB1 and PX domains. The interface of the p40phox PB1 domain for the PX domain localizes on the opposite side of that for the p67phox PB1 domain, and thus the PB1-mediated PX regulation occurs without preventing the PB1-PB1 association with p67phox.
About this Structure
2DYB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding., Honbou K, Minakami R, Yuzawa S, Takeya R, Suzuki NN, Kamakura S, Sumimoto H, Inagaki F, EMBO J. 2007 Feb 21;26(4):1176-86. Epub 2007 Feb 8. PMID:17290225
Page seeded by OCA on Thu Feb 21 17:04:01 2008
