v5.1.0.3
Glycine data from LIS
Type | Conserved_site |
Description | Microtubules are polymers of tubulin, a dimer of two 55kDa subunits, designated alpha and beta [, ]. Within the microtubule lattice, α-β heterodimers associate in a head-to-tail fashion, giving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta-tubulin toward the plus end [].For maximal rate and extent of polymerisation into microtubules, tubulin requires GTP. Two molecules of GTP are bound at different sites, termed N and E. At the E (Exchangeable) site, GTP is hydrolysed during incorporation into the microtubule. Close to the E site is an invariant region rich in glycine residues, which is found in both chains and is thought to control access of the nucleotide to its binding site [].Most species, excepting simple eukaryotes, express a variety of closely- related alpha- and beta-isotypes. A third family member, gamma tubulin, hasalso been identified in a number of species. Gamma tubulin is found at microtubule-organising centres, such as the spindle poles or the centrosome, suggesting that it is involved in minus-end nucleation of microtubule assembly [].This entry represents the glycine-rich conserved site near the E (Exchangeable) site that controls the access of the nucleotide to its binding site. |
Short Name | Tubulin_CS |