α‐, β‐, and γ‐tubulins: Sequence comparisons and structural constraints

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Abstract
Comparison of ≏ 160 α‐, β‐, and γ‐tubulins, and excluding the highly divergent C‐terminal peptide, indicates that the three subclasses have similar tertiary structures. Conserved sequences within or between the subclasses have been identified, together with the locations of known epitopes, chemical modifications, and mutations. Evidence is also reviewed concerning the identity of the GTP‐binding sites, about which residues are exposed in the assembled microtubule and at subunit:subunit interfaces. These characteristics constrain the possible tertiary structure of the tubulin subunit.