Abstract
Posttranslational modifications (PTMs) are essential mechanisms that provide chemical diversity to proteins. The additional functional and structural elements can be introduced to exceed the primary amino acid composition. PTMs impact key biological and physiological processes including cell signaling, metabolism, protein degradation and influences interactions with other macromolecules. However, characterization of the structural and functional signatures of modified proteins has been historically limited. Since defects in PTMs are linked to numerous disorders and diseases, PTMs and their modifying enzymes are considered as potential drug targets. This has fueled new initiatives to determine how PTMs affect protein structure and function. In this review, I summarize some of the major, well-studied protein PTMs and related drug targets. Since PTMs are widely used for therapeutic targets or disease markers, highlighting structural changes after PTM provides new frontiers in understanding the detailed mechanism and related drug developments.
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Acknowledgements
We thank to Dr. William Richardson and Prof. Jung Weon Lee for the informative discussions regarding the manuscript. This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (MIST) (NRF-2021M3A9D3024752 and NRF-2022R1F1A1065273) and “Leaders in Industry-university Cooperation 3.0” Project, supported by the Ministry of Education and National Research Foundation of Korea.
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Funding was provided by National Research Foundation of Korea, (Grant No. 2021M3A9D3024752),National Research Foundation of Korea, (Grant No. 2020R1G1A1100821), Ministry of Education and National Research Foundation of Kore, Leaders in INdustry-university Cooperation + .
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Kim, H.J. Minor structural changes, major functional impacts: posttranslational modifications and drug targets. Arch. Pharm. Res. 45, 693–703 (2022). https://doi.org/10.1007/s12272-022-01409-y
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DOI: https://doi.org/10.1007/s12272-022-01409-y