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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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Publisher copy:
10.1039/c8cc01009a

Authors


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Role:
Author
ORCID:
0000-0002-7958-2271
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
ORCID:
0000-0002-5615-6237
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Role:
Author
ORCID:
0000-0002-0814-5074
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Funding agency for:
Poater, J
Grant:
CTQ2016-77558-R
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Funding agency for:
Mecinović, J
Grant:
ChemEpigen-715691
Netherlands Organization for Scientific Research More from this funder
Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Chemical Communications Journal website
Volume:
54
Issue:
19
Pages:
2409-2412
Publication date:
2018-02-09
Acceptance date:
2018-02-09
DOI:
EISSN:
1364-548X
ISSN:
1359-7345
Pmid:
29457186
Source identifiers:
826247
Language:
English
Keywords:
Pubs id:
pubs:826247
UUID:
uuid:8abc116c-a1a0-4510-9a94-d92329f291ac
Local pid:
pubs:826247
Deposit date:
2018-04-12

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