Fig. 2
From: Epsin and Sla2 form assemblies through phospholipid interfaces
Crystal structure of the ENTH2/PIP2 complex reveals an allosteric-binding mechanism. a Ribbon diagram of the ENTH2α0 (cyan) and ENTH2Noα0 dimer (blue) building block. N-terminal regions are colored (ENTH2α0, yellow; ENTH2Noα0, orange). PIP2 sitting in the interface between ENTH2 molecules is shown as spheres. b Superposition of the ENTH/IP3 epsin-1 complex (dark blue) and the ENTH2/PIP2 complex (yellow). The N-terminal α0 is colored (ENTH2/PIP2, yellow; ENTH/IP3, orange), the inositol head groups are shown as sticks. c Superimposition of the ENTH2/PIP2 dimer (blue/cyan) and the ENTH1 dimer (green/palegreen) shown as a ribbon diagram. The α0 helix of ENTH1 is oriented similarly to α0 of ENTH2α0. d Surface presentation of the ENTH2/PIP2 complex showing that unfolded N-termini of ENTH2 are in plane with the lipid tail of the PIP2 molecules (two ENTH2α0/ENTH2Noα0 building blocks, cyan/blue and magenta/violet; PIP2, spheres; N-termini for empty ENTH2, yellow and orange; Tyr 16, Arg 24, Arg 62 and His 72 of ENTH2Noα0 with empty PIP2-binding pocket, red)
