Post-translational modifications in the Protein Data Bank

TY - JOUR

T1 - Post-translational modifications in the Protein Data Bank

AU - Schofield, Lucy C

AU - Dialpuri, Jordan S

AU - Murshudov, Garib N

AU - Agirre, Jon

N1 - Publisher Copyright: © 2024 International Union of Crystallography. All rights reserved.

PY - 2024/9/1

Y1 - 2024/9/1

N2 - 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.

AB - 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.

KW - acetylation

KW - glycosylation

KW - phosphorylation

KW - post-translational modifications

KW - Protein Data Bank

UR - http://www.scopus.com/inward/record.url?scp=85204017265&partnerID=8YFLogxK

U2 - 10.1107/S2059798324007794

DO - 10.1107/S2059798324007794

M3 - Article

C2 - 39207896

SN - 2059-7983

VL - 80

SP - 647

EP - 660

JO - Acta crystallographica. Section D, Structural biology

JF - Acta crystallographica. Section D, Structural biology

IS - Pt 9

M1 - D80

ER -