1oey
From Proteopedia
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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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