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. 2009 Apr 30;41(4):217–225. doi: 10.3858/emm.2009.41.4.058

Figure 2.

Figure 2

Phosphorylation of p47phox induces conformational changes and changes domains interactions. In resting state the two p47phox-SH3 domains interact with the C-terminal region AIR to keep the protein in an auto-inhibited state. Upon activation, p47phox is phosphorylated, this phosphorylation induces conformational changes allowing the binding of the cryptic SH3 domains to the proline-rich region (PRR) of p22phox and PX domain to phosphatidylinositol 3,4-biphosphate (PI3,4P), phosphatidic acid (PA) and moesin.