An idealized membrane binding domain is shown in the same color scheme used in Fig. 1.

Surfaces are rendered with hydrophobic residues in green, basic in blue, acidic in red, and uncharged polar in white. The yellow line marks the top of the polar interface region of the bilayer, and the green line marks the top of the hydrocarbon core of the bilayer. The C1B domain of PKC-δ bound to phorbol 13-acetate (1PTR) [11] was docked to the membrane on the basis of structural modeling and solution NMR of the related PKC-γ C1B domain [27]. The C2 domain of PKC-α (1DSY) [39] was docked on the basis of FRET and EPR analysis [78]. The PH domain of PLC-δ (1MAI) [13] was docked on the basis of structural modeling. The FYVE domain of Vps27 (1VFY) [56], with PI(3)P docked on the basis of its binding site in EEA1 [58], was docked to the membrane based on structural and electrostatic modeling [74]. The PX domain of p40^phox bound to PI(3)P (1H6H) [62] was docked on the basis of structural modeling and demonstrated membrane penetration [77]. The ENTH domain of epsin (1HOA) [63] bound to PI(4,5)P₂ was docked on the basis of structural modeling and demonstrated membrane penetration [79]. The amphiphysin BAR domain (1URU) [68] was docked to a curved membrane surface based on shape complementarity. Phospholipid and phorbol ester tail moieties were modeled arbitrarily except for the PX domain, where the crystallized conformation is shown.