Supplementary Figure 5: Comparison of the phosphoinositide-binding pocket of Sky1–353 with other typical phosphoinositide-binding domains.
From: Skywalker-TBC1D24 has a lipid-binding pocket mutated in epilepsy and required for synaptic function
Structures of representatives of well-established phosphoinositide-binding domains (ENTH, PX, FYVE and PH) in complex with a phosphoinositide head group are shown in electrostatic surface representation and are compared to the Sky1-353 structure in complex with IP3. The boxes show a close-up of the phosphoinositide binding pocket in cartoon representation with the phosphoinositide head group and the interacting residues shown as sticks. The structures that are shown are: the TBC domain of Sky bound to IP3 (this study), the ENTH domain of epsin bound to IP3 (pdb 1H0A; Ford, M. G. J. et al., Nature 419, 361–366, 2002), the PX domain of P40phox bound to dibutanoyl IP2 (pdb 1H6H; Bravo, J. et al., Mol. Cell 8, 829–39, 2001), the FYVE domain of EEA1 bound to IP2 (pdb 1JOC; Dumas, J. J. et al., Mol. Cell 8, 947–58, 2001), the PH domain of PLC-δ1 bound to IP3 (pdb 1MAI; Ferguson, K. M. et al., Cell 83, 1037–1046, 1995) and the PH domain of spectrin bound to IP3 (pdb 1BTN; Hyvönen, M. et al., EMBO J. 14, 4676–85, 1995).
