TABLE 3.
Predicted coiled-coil start sites, actual start sites, and the corresponding probabilities of the residue being in a coiled-coil according to MARCOIL and COILS using the 28-residue window
| Kinesin | Observed start residuea | MARCOIL | COILS-28 | Predicted start residueb | MARCOIL | COILS-28 |
|---|---|---|---|---|---|---|
| Kinesin-1 | Ala-345 | 0.815 | 1.000 | Ala-345 | 0.815 | 1.000 |
| KIF3A | Pro-355 | 0.432 | 0.846 | Leu-360 | 0.853 | 0.846 |
| KIF3C | Pro-377 | 0.086 | 0.056 | Leu-382 | 0.578 | 0.056 |
| Eg5 | Lys-371 | 0.694 | 1.000 | Ile-375 | 0.945 | 1.000 |
| CENP-E | Asp-341 | 0.828 | 1.000 | Leu-345 | 0.978 | 1.000 |
| KIF3A-kinesin-1 (hybrid) | Ala-358 (A345-2)c | 0.416 | 1.000 | Kinesin-1-Ala-345 | 0.728 | 1.000 |
| Leu-359 (A345-1)c | 0.546 | 1.000 |
a Observed start residues are determined using the first residue in a helical conformation in the crystal structures of the neck-linker protein defined as helix as determined by Dictionary of Secondary Structure of Proteins.
b Predicted start residue as determined in Ref. 36. This start was assumed in earlier kinetic studies of kinesins to determine the influence of the neck-linker length.
c The KIF3A neck-linker residue where the coiled coil starts is shown first, followed by the corresponding position in kinesin-1 relative to the kinesin-1 α7 start.