Interaction of tubulin with ribose-modified analogs of GTP and GDP : Evidence for two mutually exclusive exchangeable nucleotide binding sites ( tubulin polymerization / nucleotide hydrolysis / exchangeable GTP binding site / nucleotide inhibition )

@inproceedings{HamelInteractionOT,
  title={Interaction of tubulin with ribose-modified analogs of GTP and GDP : Evidence for two mutually exclusive exchangeable nucleotide binding sites ( tubulin polymerization / nucleotide hydrolysis / exchangeable GTP binding site / nucleotide inhibition )},
  author={Ernest Hamel and Chii Mei Lin}
}
Interactions of tubulin with a number of guanine nucleotides modified at the 2' and 3' ribose hydroxyls were examined. Deoxy analogs of GTP were equal or superior to GTP in supporting tubulin polymerization, but analogs bearing either methyl or phosphate groups on the hydroxyls had significantly reduced ability to support polymerization. These substituted… CONTINUE READING