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Article

Structural Basis of Telomerase Inhibition by the Highly Specific BIBR1532.

Structure (London, England : 1993) - 6 Oct 2015

Bryan Christopher, Rice Cory, Hoffman Hunter, Harkisheimer Michael, Sweeney Melanie, Skordalakes Emmanuel

Abstract excerpt

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...

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Identifiers

PMID: 26365799
DOI: 10.1016/j.str.2015.08.006
PMCID: PMC4598299

Genes

TERT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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