Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p

The FYVE domains' interaction with the phosphatidylinositol three-phosphate membranes controls membrane trafficking and signalling pathways. Study of the FYVE domain structure revealed that this amino acid region is composed of two antiparallel beta sheets and an L helix stabilized by two Zn2+-binding clusters. It was also observed that the tip of the FYVE domain has basic and hydrophobic surfaces that promote nonspecific interactions with the phospholipid bilayer.