The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation
Open accessAbstract
ALKBH5 is a 2-oxoglutarate (2OG) and ferrous iron-dependent nucleic acid oxygenase (NAOX) that catalyzes the demethylation of N6-methyladenine in RNA. ALKBH5 is upregulated under hypoxia and plays a role in spermatogenesis. We describe a crystal structure of human ALKBH5 (residues 66–292) to 2.0 Å resolution. ALKBH566–292 has a double-stranded β-helix core fold as observed in other 2OG and iron-dependent oxygenase family members. The active site metal is octahedrally coordinated by an HXD…H motif (comprising residues His204, Asp206 and His266) and three water molecules. ALKBH5 shares a nucleotide recognition lid and conserved active site residues with other NAOXs. A large loop (βIV–V) in ALKBH5 occupies a similar region as the L1 loop of the fat mass and obesity-associated protein that is proposed to confer single-stranded RNA selectivity. Unexpectedly, a small molecule inhibitor, IOX3, was observed covalently attached to the side chain of Cys200 located outside of the active site. Modelling substrate into the active site based on other NAOX–nucleic acid complexes reveals conserved residues important for recognition and demethylation mechanisms. The structural insights will aid in the development of inhibitors selective for NAOXs, for use as functional probes and for therapeutic benefit.
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Phaser crystallographic software
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Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons
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N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO
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ALKBH5 Is a Mammalian RNA Demethylase that Impacts RNA Metabolism and Mouse Fertility
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Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
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Structural studies on human 2-oxoglutarate dependent oxygenases
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Cited by
The proteins of mRNA modification: writers, readers, and erasers
Flamand, M. N., Tegowski, M., & Meyer, K. D. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052521-035330 · Cited by 164
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Metadata
- Authors
- Aik, W., Scotti, J. S., Choi, H., Gong, L., Demetriades, M., Schofield, C. J., & McDonough, M. A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-01-30
- Volume
- 42
- Issue
- 7
- Pages
- 4741-4754
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2167149089
- Cited by
- 244
- References
- 8
- FWCI
- 4.02
- Type
- journal article
- Language
- en
- Open access
- gold
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- Aik, W., Scotti, J. S., Choi, H., Gong, L., Demetriades, M., Schofield, C. J., & McDonough, M. A. (2014). Structure of human RNA N 6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation. Nucleic Acids Research. https://doi.org/10.1093/nar/gku085
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