 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
journal menu
![[Figure 6]](dw5063fig6mag.jpg)
|
|
Figure 6
Comparison of current models for Eg5 and Kif15 MT crosslinking and function. Under physiological conditions homotetrameric Eg5 (blue) interacts with antiparallel MTs through two distinct binding sites in its motor and tail domains (two in the motor and two in the tail for each MT it crosslinks), and slides them apart (Weinger et al., 2011  ). Dimeric Kif15 (green) works predominantly on K-fibres (Sturgill & Ohi, 2013). It forms a complex with TPX2 (pink) via its tail domain to bind statically to one MT while moving along a second (Tanenbaum et al., 2009). It can also interacts with chromosomes via its interaction wit FHA domain of Ki-67 (Sueishi et al., 2000). The stoichiometry of the Kif15–Ki-67 and the Kif15–TPX2 complex is unknown. |
![[Figure 6]](dw5063fig6.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
