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Figure 2.
(a,b) Surface representations of HEC1_CH in the orientations
of Figure 1a,b, respectively, colored by degree of conservation
(dark blue, most conserved; white, least conserved), showing
that the potential microtubule-binding surface is conserved
across species. (c,d) Surface representations showing
electrostatic potential of HEC1_CH and EB1 microtubule-binding
domain, in the orientations of Figure 1b,d, respectively. Red to
blue, -15 k[b]T to +15 k[b]T, as calculated by Delphi^49. (e)
Multiple sequence alignment for Ndc80/HEC1 and EB1 CH domain
(bottom), generated with CLUSTAL W^50. Secondary structural
elements derived from the crystal structure are colored as in
Figure 1a. Number of initial residue for each homolog is shown
after species name. Residues are colored by degree of
conservation: white letters on dark blue background, identical;
blue on blue-gray, strongly conserved; light blue on white,
weakly conserved. Lys89 of EB1, which is required for
microtubule binding, is boxed in red.
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