Schofield, Lucy C, Dialpuri, Jordan S, Murshudov, Garib N et al. (1 more author) (2024) Post-translational modifications in the Protein Data Bank. Acta crystallographica. Section D, Structural biology. D80. pp. 647-660. ISSN 2059-7983
Abstract
Proteins frequently undergo covalent modification at the post-translational level, which involves the covalent attachment of chemical groups onto amino acids. This can entail the singular or multiple addition of small groups, such as phosphorylation; long-chain modifications, such as glycosylation; small proteins, such as ubiquitination; as well as the interconversion of chemical groups, such as the formation of pyroglutamic acid. These post-translational modifications (PTMs) are essential for the normal functioning of cells, as they can alter the physicochemical properties of amino acids and therefore influence enzymatic activity, protein localization, protein-protein interactions and protein stability. Despite their inherent importance, accurately depicting PTMs in experimental studies of protein structures often poses a challenge. This review highlights the role of PTMs in protein structures, as well as the prevalence of PTMs in the Protein Data Bank, directing the reader to accurately built examples suitable for use as a modelling reference.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Publisher Copyright: © 2024 International Union of Crystallography. All rights reserved. |
Keywords: | acetylation,glycosylation,phosphorylation,post-translational modifications,Protein Data Bank |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Funding Information: | Funder Grant number BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL) BB/Y009339/1, BB/Y00888X/1 |
Depositing User: | Pure (York) |
Date Deposited: | 03 Sep 2024 13:10 |
Last Modified: | 16 Oct 2024 20:07 |
Published Version: | https://doi.org/10.1107/S2059798324007794 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1107/S2059798324007794 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:216797 |