Structural Basis of Telomerase Inhibition by the Highly Specific BIBR1532.

@article{Bryan2015StructuralBO,
  title={Structural Basis of Telomerase Inhibition by the Highly Specific BIBR1532.},
  author={Christopher Bryan and Cory T Rice and Hunter Hoffman and Michael J Harkisheimer and Melanie Sweeney and Emmanuel Skordalakes},
  journal={Structure},
  year={2015},
  volume={23 10},
  pages={1934-1942}
}
BIBR1532 is a highly specific telomerase inhibitor, although the molecular basis for inhibition is unknown. Here we present the crystal structure of BIBR1532 bound to Tribolium castaneum catalytic subunit of telomerase (tcTERT). BIBR1532 binds to a conserved hydrophobic pocket (FVYL motif) on the outer surface of the thumb domain. The FVYL motif is near TRBD residues that bind the activation domain (CR4/5) of hTER. RNA binding assays show that the human TERT (hTERT) thumb domain binds the P6.1… CONTINUE READING
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