Journal article
Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins
- Abstract:
- Histone Nε-lysine methylation is a widespread posttranslational modification that is specifically recognised by a diverse class of Nε-methyllysine binding reader proteins. Combined thermodynamic data, molecular dynamics simulations, and quantum chemical studies reveal that reader proteins efficiently bind trimethylornithine and trimethylhomolysine, the simplest Nε-trimethyllysine analogues that differ in the length of the side chain.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Access Document
- Files:
-
-
(Preview, Accepted manuscript, pdf, 362.1KB, Terms of use)
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- Publisher copy:
- 10.1039/c8cc01009a
Authors
+ European Research Council
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- Funding agency for:
- Mecinović, J
- Grant:
- ChemEpigen-715691
+ Ministry of Economy and Competitiveness (Spain)
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- Funding agency for:
- Poater, J
- Grant:
- CTQ2016-77558-R
- Publisher:
- Royal Society of Chemistry
- Journal:
- Chemical Communications More from this journal
- Volume:
- 54
- Issue:
- 19
- Pages:
- 2409-2412
- Publication date:
- 2018-02-09
- Acceptance date:
- 2018-02-09
- DOI:
- EISSN:
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1364-548X
- ISSN:
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1359-7345
- Pmid:
-
29457186
- Language:
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English
- Keywords:
- Pubs id:
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pubs:826247
- UUID:
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uuid:8abc116c-a1a0-4510-9a94-d92329f291ac
- Local pid:
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pubs:826247
- Source identifiers:
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826247
- Deposit date:
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2018-04-12
Terms of use
- Copyright holder:
- Temimi, et al
- Copyright date:
- 2018
- Notes:
- This is the accepted manuscript version of the article. The final version is available online from the Royal Society of Chemistry at: https://doi.org/10.1039/c8cc01009a
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