1OEY

Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase

Summary for 1OEY

• Entry DOI: 10.2210/pdb1oey/pdb
• Related: 1E96 1H6H 1HH8 1IP9 1IPG 1K4U
• Descriptor: NEUTROPHIL CYTOSOL FACTOR 2, NEUTROPHIL CYTOSOL FACTOR 4 (3 entities in total)
• Functional Keywords: immune system, pb1 heterodimer-complex, nadph oxidase, pb1 domain, heterodimerization
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: P19878; Cytoplasm, cytosol : Q15080
• Total number of polymer chains: 8
• Total formula weight: 91155.61

Authors

Wilson, M.I.,Gill, D.J.,Perisic, O.,Quinn, M.T.,Williams, R.L. (deposition date: 2003-04-02, release date: 2003-07-29, Last modification date: 2024-10-16)

Primary citation

Wilson, M.I.,Gill, D.J.,Perisic, O.,Quinn, M.T.,Williams, R.L.
Pb1 Domain-Mediated Heterodimerization in Nadph Oxidase and Signaling Complexes of Atypical Protein Kinase C with Par6 and P62
Mol.Cell, 12:39-, 2003

PubMed Abstract: 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.

PubMed: 12887891
DOI: 10.1016/S1097-2765(03)00246-6

Experimental method

X-RAY DIFFRACTION (2 Å)