Fig. 1.
Crystal structures of the CAP-Gly-1 and CAP-Gly-2 domains. (a) Domain organization of the CLIP-170 dimer. The N-terminal CAP-Gly domains directly bind MT/tubulin. This binding is autoinhibited by the C-terminal zinc knuckle domains, which also serve to recruit dynein by interacting with p150Glued and LIS1. (b) Ribbon drawings of the crystal structure of the CLIP-170 CAP-Gly-1 domain (Left), electrostatic potentials on the front molecular surface in the same molecular orientation (Center), and a 180° rotated image (Right). The region corresponding to the GKNDG motif is circled with yellow broken lines. (c) Same figures as in b but for the CLIP-170 CAP-Gly-2 domain. Electrostatic potentials of the front surfaces of the CAP-Gly domains of p150Glued (PDB ID, 2HL3) (d), CYLD (1IXD) (e), and F53.43 (1LPL) (f).