2dyb

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[[Image:2dyb.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2dyb| PDB=2dyb | SCENE= }}
{{STRUCTURE_2dyb| PDB=2dyb | SCENE= }}
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'''The crystal structure of human p40(phox)'''
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===The crystal structure of human p40(phox)===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_17290225}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17290225 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17290225}}
==About this Structure==
==About this Structure==
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[[Category: Honbou, K.]]
[[Category: Honbou, K.]]
[[Category: Nadph oxidase]]
[[Category: Nadph oxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:36:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:55:49 2008''

Revision as of 00:55, 29 July 2008

Image:2dyb.png

Template:STRUCTURE 2dyb

The crystal structure of human p40(phox)

Template:ABSTRACT PUBMED 17290225

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

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