Abstract
G-quadruplexes (G4s) are non-canonical DNA secondary structures. The identification of selective tools to probe individual G4s over the ∼700 000 found in the human genome is key to unravel the biological significance of specific G4s. We took inspiration from a crystal structure of the bovine DHX36 helicase bound to the G4 formed in the promoter region of the oncogene c-MYC to identify a short peptide that preferentially binds MYC G4 with nM affinity over a small panel of parallel and non-parallel G4s tested.
Highlights
Aisling Minard, ‡ab Danielle Morgan,‡c Federica Raguseo,a Anna Di Porzio, ad Denise Liano, ab Andrew G
The identification of selective tools to probe individual G4s over the B700 000 found in the human genome is key to unravel the biological significance of specific G4s
We took inspiration from a crystal structure of the bovine DHX36 helicase bound to the G4 formed in the promoter region of the oncogene c-MYC to identify a short peptide that preferentially binds MYC G4 with nM affinity over a small panel of parallel and non-parallel G4s tested
Summary
Aisling Minard, ‡ab Danielle Morgan,‡c Federica Raguseo,a Anna Di Porzio, ad Denise Liano, ab Andrew G. We took inspiration from a crystal structure of the bovine DHX36 helicase bound to the G4 formed in the promoter region of the oncogene c-MYC to identify a short peptide that preferentially binds MYC G4 with nM affinity over a small panel of parallel and non-parallel G4s tested.
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