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2N21

Solution structure of complex between DNA G-quadruplex and G-quadruplex recognition domain of RHAU

Summary for 2N21
Entry DOI10.2210/pdb2n21/pdb
NMR InformationBMRB: 25582
DescriptorATP-dependent RNA helicase DHX36, DNA (5'-D(*TP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*TP*GP*GP*GP*T)-3') (2 entities in total)
Functional Keywordshydrolase-dna complex, hydrolase/dna
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: Q9H2U1
Total number of polymer chains2
Total formula weight8091.47
Authors
Heddi, B.,Cheong, V.V.,Martadinata, H.,Phan, A.T. (deposition date: 2015-04-25, release date: 2015-07-29, Last modification date: 2024-05-15)
Primary citationHeddi, B.,Cheong, V.V.,Martadinata, H.,Phan, A.T.
Insights into G-quadruplex specific recognition by the DEAH-box helicase RHAU: Solution structure of a peptide-quadruplex complex.
Proc.Natl.Acad.Sci.USA, 112:9608-9613, 2015
Cited by
PubMed Abstract: Four-stranded nucleic acid structures called G-quadruplexes have been associated with important cellular processes, which should require G-quadruplex-protein interaction. However, the structural basis for specific G-quadruplex recognition by proteins has not been understood. The DEAH (Asp-Glu-Ala-His) box RNA helicase associated with AU-rich element (RHAU) (also named DHX36 or G4R1) specifically binds to and resolves parallel-stranded G-quadruplexes. Here we identified an 18-amino acid G-quadruplex-binding domain of RHAU and determined the structure of this peptide bound to a parallel DNA G-quadruplex. Our structure explains how RHAU specifically recognizes parallel G-quadruplexes. The peptide covers a terminal guanine base tetrad (G-tetrad), and clamps the G-quadruplex using three-anchor-point electrostatic interactions between three positively charged amino acids and negatively charged phosphate groups. This binding mode is strikingly similar to that of most ligands selected for specific G-quadruplex targeting. Binding to an exposed G-tetrad represents a simple and efficient way to specifically target G-quadruplex structures.
PubMed: 26195789
DOI: 10.1073/pnas.1422605112
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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