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Figure 1.
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
p150^Glued 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 p150^Glued (PDB ID, 2HL3) (d), CYLD
(1IXD) (e), and F53.43 (1LPL) (f).
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