Article ; Online: Modus operandi: Chromatin recognition by α-helical histone readers.
Structure (London, England : 1993)
2023 Volume 32, Issue 1, Page(s) 8–17
Abstract: Histone reader domains provide a mechanism for sensing states of coordinated nuclear processes marked by histone proteins' post-translational modifications (PTMs). Among a growing number of discovered histone readers, the 14-3-3s, ankyrin repeat domains ( ...
Abstract | Histone reader domains provide a mechanism for sensing states of coordinated nuclear processes marked by histone proteins' post-translational modifications (PTMs). Among a growing number of discovered histone readers, the 14-3-3s, ankyrin repeat domains (ARDs), tetratricopeptide repeats (TPRs), bromodomains (BRDs), and HEAT domains are a group of domains using various mechanisms to recognize unmodified or modified histones, yet they all are composed of an α-helical fold. In this review, we compare how these readers fold to create protein domains that are very diverse in their tertiary structures, giving rise to intriguing peptide binding mechanisms resulting in vastly different footprints of their targets. |
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MeSH term(s) | Chromatin ; Histones/metabolism ; Protein Processing, Post-Translational ; Protein Domains |
Chemical Substances | Chromatin ; Histones |
Language | English |
Publishing date | 2023-11-02 |
Publishing country | United States |
Document type | Journal Article ; Review |
ZDB-ID | 1213087-4 |
ISSN | 1878-4186 ; 0969-2126 |
ISSN (online) | 1878-4186 |
ISSN | 0969-2126 |
DOI | 10.1016/j.str.2023.10.008 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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