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Fig. 3. Structure of SNX9. (A) Ribbon diagram of the crystal structure of the membrane-remodeling yoke-PX-BAR dimer [Protein Data Bank (PDB) entry 2RAK], color-coded as in Fig. 2. In the upper structure, the membrane-binding surface is towards the viewer; the lower structure is a side view. Phosphoinositides (green) are bound to the canonical phosphoinositide-binding pockets. (B) Size comparison of SNX9 and dynamin. To the left is the full-length dimer of SNX9 with the electrostatic surface potential shown in red (negative charge) and blue (positive charge). The SH3-domain structure is from the PDB entry 2ENM and the LC domain is randomly depicted to denote its flexibility. To the right is a schematic model of dimeric dynamin that is drawn roughly to scale with SNX9. The model is based on cryoelectron micrographs (Mears et al., 2007). The GTPase domains of dynamin are the large balls at the top of the structure and the membrane-binding PH domains are at the bottom. The proline-rich domains (PRDs) are depicted as unstructured ribbons that emanate from the central region, which comprises the middle domains and the GTPase effector domains. The figure shows that the SNX9 SH3 domain and the dynamin PRD can interact with each other above the bulk of either protein and that SNX9 can reach out above dynamin to enable additional interactions, such as with N-WASP, while it is assembled on the membrane surface.
