Ontology highlight
ABSTRACT:
SUBMITTER: Bryan C
PROVIDER: S-EPMC4598299 | biostudies-literature | 2015 Oct
REPOSITORIES: biostudies-literature
Structure (London, England : 1993) 20150910 10
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 s ...[more]