Sequence alignment of EBs and structure of the EBH domain.

<p>(<b>A</b>) Sequence alignment of full length human EB1 (accession number AAC09471) and EB3 (accession number BAA82958). The N-terminal domain, linker, coiled coil, EBH domain and tail region are indicated. The arrowhead highlights the isoleucine residue (Ile224 in EB1 and Ile233 in EB3), which was mutated to alanine to create EB monomers. (B) Two views 90° apart of the EBH domain of EB1 showing the core packing interactions of Ile224 and Ile242 (in sphere representation). Monomers A and B of the EBH domain are colored in grey and yellow, respectively, and are shown in cartoon representation. Residues of monomer B are indicated by a prime.