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. Author manuscript; available in PMC: 2018 Oct 1.
Published in final edited form as: FEBS J. 2017 Aug 30;284(20):3381–3391. doi: 10.1111/febs.14197

Fig. 1.

Fig. 1

Structure and function of the intrinsically disordered GTPase binding domain (GBD) in the Wiskott-Aldrich Syndrome protein (WASP). (a) Domain organization of WASP and intramolecular and intermolecular interactions of the GBD, comprising a basic region (blue box), a Cdc42/Rac1 interactive binding motif (CRIB; yellow box), and a downstream sequence (green box). Cdc42 can dislodge from the GBD the VCA domain (V: verprolin-homology region; C: cofilin-homology region; and A: acidic region), allowing the latter to interact with G-actin and Arp2/3. (b) Autoinhibiting interaction between the GBD (green) and the C helix (cyan); structure from Protein Data Bank (PDB) entry 1EJ5. (c) Extended structure and intermolecular interaction of the WASP GBD on the surface of Cdc42 (PDB entry 1CEE). The left panel highlights the acidic Cdc42 surface interacting with the WASP BR; the right panel displays a bound nucleotide to indicate the position of the fluorophore used for monitoring binding kinetics.