Burns R G
Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, United Kingdom.
Cell Motil Cytoskeleton. 1991;20(3):181-9. doi: 10.1002/cm.970200302.
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.
将160种α-、β-和γ-微管蛋白进行比对，并排除高度分化的C端肽段，结果表明这三个亚类具有相似的三级结构。已确定亚类内部或之间的保守序列，以及已知表位、化学修饰和突变的位置。还综述了关于GTP结合位点的一致性的证据，即哪些残基在组装好的微管中以及在亚基与亚基界面处是暴露的。这些特征限制了微管蛋白亚基可能的三级结构。
