Figure 3

Coiled-coil crystal structure of NDEL1 with known post-translational modifications mapped.

Only three known PTMs map onto the crystal structure of the NDEL1 coiled-coil domain fragment (residues 8–167; PDB ID: 2V71); these side-chains are shown in green and labeled on cartoon representations of the NDEL1 crystal structure, parallel dimer (top panel) and anti-parallel tetramer (bottom panel) (81); N- and C-termini for each chain and regions that facilitate dimerization and tetramerization are indicated. The essential LIS1-binding region on NDEL1 114–133 (96) is also shown (pink). Phosphorylation of NDE1 at T131 (directly equivalent to T132 of NDEL1) reduces its ability to interact with LIS1 (86). It can therefore be hypothesized that phosphorylation of T132 and/or S135 of NDEL1 may have similar effects on LIS1-binding. The Y87 site is highly solvent-exposed on the dimerization domain of coiled-coil structure and is thus readily accessible to kinases.

© De Gruyter