1oey: Difference between revisions

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[[Image:1oey.png|left|200px]]

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~~'''~~HETERODIMER OF P40PHOX AND P67PHOX PB1 DOMAINS FROM HUMAN NADPH OXIDASE~~'''~~

===HETERODIMER OF P40PHOX AND P67PHOX PB1 DOMAINS FROM HUMAN NADPH OXIDASE===

~~==Overview==~~

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Maximal activation of NADPH oxidase requires formation of a complex between the p40(phox) and p67(phox) subunits via association of their PB1 domains. We have determined the crystal structure of the p40(phox)/p67(phox) PB1 heterodimer, which reveals that both domains have a beta grasp topology and that they bind in a front-to-~~back arrangement through conserved electrostatic interactions between an acidic OPCA motif on p40(phox) and basic residues in p67(phox).~~ The ~~structure enabled us to identify residues critical for heterodimerization among other members of the PB1 domain family~~, ~~including~~ the ~~atypical protein kinase C zeta (PKC zeta) and its partners Par6 and p62 (ZIP, sequestosome). Both Par6 and p62 use their basic "back"~~ to ~~interact with~~ the ~~OPCA motif~~ on ~~the "front" of the PKC zeta~~. ~~Besides heterodimeric interactions~~, ~~some PB1 domains, like~~ the ~~p62 PB1, can make homotypic front~~-to-~~back arrays.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12887891}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12887891 is the PubMed ID number.

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==About this Structure==

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[[Category: Nadph oxidase]]

[[Category: Pb1 domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 03~~:45:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:14:20 2008''

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-[[Image:1oey.jpg|left|200px]]
+{{Seed}}
+[[Image:1oey.png|left|200px]]
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 {{STRUCTURE_1oey|  PDB=1oey  |  SCENE=  }}
-'''HETERODIMER OF P40PHOX AND P67PHOX PB1 DOMAINS FROM HUMAN NADPH OXIDASE'''
+===HETERODIMER OF P40PHOX AND P67PHOX PB1 DOMAINS FROM HUMAN NADPH OXIDASE===
-==Overview==
+<!--
-Maximal activation of NADPH oxidase requires formation of a complex between the p40(phox) and p67(phox) subunits via association of their PB1 domains. We have determined the crystal structure of the p40(phox)/p67(phox) PB1 heterodimer, which reveals that both domains have a beta grasp topology and that they bind in a front-to-back arrangement through conserved electrostatic interactions between an acidic OPCA motif on p40(phox) and basic residues in p67(phox). The structure enabled us to identify residues critical for heterodimerization among other members of the PB1 domain family, including the atypical protein kinase C zeta (PKC zeta) and its partners Par6 and p62 (ZIP, sequestosome). Both Par6 and p62 use their basic "back" to interact with the OPCA motif on the "front" of the PKC zeta. Besides heterodimeric interactions, some PB1 domains, like the p62 PB1, can make homotypic front-to-back arrays.
+The line below this paragraph, {{ABSTRACT_PUBMED_12887891}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12887891 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12887891}}
 ==About this Structure==
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 [[Category: Nadph oxidase]]
 [[Category: Pb1 domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:45:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:14:20 2008''