Alpha-, beta-, and gamma-tubulins: sequence comparisons and structural constraints.
Comparison of congruent to 160 alpha-, beta-, and gamma-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.
Burns
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Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, United Kingdom.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D008870:Microtubules / Q000378:metabolism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D014404:Tubulin / Q000737:chemistry* / Q000145:classification / Q000235:genetics
D005656:Fungal Proteins; D014404:Tubulin; D006160:Guanosine Triphosphate