| Literature DB >> 34624071 |
Kendra R Vann1, Yashavantha L Vishweshwaraiah2, Nikolay V Dokholyan2,3, Tatiana G Kutateladze1.
Abstract
Methylation of lysine residues plays crucial roles in a wide variety of cell signaling processes. While the biological importance of recognition of methylated histones by reader domains in the cell nucleus is well established, the processes associated with methylation of non-histone proteins, particularly in the cytoplasm of the cell, are not well understood. Here, we describe a search for potential methyllysine readers using a rapid structural motif-mining algorithm Erebus, the PDB database, and knowledge of the methyllysine binding mechanisms.Entities:
Keywords: aromatic cage; binding; methylation; structure
Mesh:
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Year: 2021 PMID: 34624071 PMCID: PMC9416871 DOI: 10.1042/BCJ20210106
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.766