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Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins

Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4673829

Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins

About this item

Full title

Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2015-11, Vol.6 (1), p.8911, Article 8911

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

A large number of structurally diverse epigenetic reader proteins specifically recognize methylated lysine residues on histone proteins. Here we describe comparative thermodynamic, structural and computational studies on recognition of the positively charged natural trimethyllysine and its neutral analogues by reader proteins. This work provides ex...

Alternative Titles

Full title

Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4673829

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4673829

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms9911

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