1oey
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Maximal activation of NADPH oxidase requires formation of a complex | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Gill, D | + | [[Category: Gill, D J.]] |
[[Category: Perisic, O.]] | [[Category: Perisic, O.]] | ||
| - | [[Category: Quinn, M | + | [[Category: Quinn, M T.]] |
| - | [[Category: Williams, R | + | [[Category: Williams, R L.]] |
| - | [[Category: Wilson, M | + | [[Category: Wilson, M I.]] |
[[Category: heterodimerization]] | [[Category: heterodimerization]] | ||
[[Category: nadph oxidase]] | [[Category: nadph oxidase]] | ||
[[Category: pb1 domain]] | [[Category: pb1 domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:55 2008'' |
Revision as of 12:17, 21 February 2008
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HETERODIMER OF P40PHOX AND P67PHOX PB1 DOMAINS FROM HUMAN NADPH OXIDASE
Contents |
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.
Disease
Known disease associated with this structure: Chronic granulomatous disease due to deficiency of NCF-2 OMIM:[608515]
About this Structure
1OEY is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62., Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL, Mol Cell. 2003 Jul;12(1):39-50. PMID:12887891
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