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Open Access Green as soon as Postprint is submitted to ZB.
Studying weak and dynamic interactions of posttranslationally modified proteins using expressed protein ligation.
ACS Chem. Biol. 9, 347-352 (2014)
Many cellular processes are regulated by posttranslational modifications that are recognized by specific domains in protein binding partners. These interactions are often weak, thus allowing a highly dynamic and combinatorial regulatory network of protein-protein interactions. We report an efficient strategy that overcomes challenges in structural analysis of such a weak transient interaction between the Tudor domain of the Survival of Motor Neuron (SMN) protein and symmetrically dimethylated arginine (sDMA). The posttranslational modification is chemically introduced and covalently linked to the effector module by a one-pot expressed protein ligation (EPL) procedure also enabling segmental incorporation of NMR-active isotopes for structural analysis. Covalent coupling of the two interacting moieties shifts the equilibrium to the bound state, and stoichiometric interactions are formed even for low affinity interactions. Our approach should enable the structural analysis of weak interactions by NMR or X-ray crystallography to better understand the role of posttranslational modifications in dynamic biological processes.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Smn Tudor Domain; Resolution X-ray; Chemical-synthesis; Arginine Residues; Semisynthesis; Photocontrol; Binding; Site
ISSN (print) / ISBN
1554-8929
e-ISSN
1554-8937
Journal
ACS Chemical Biology
Quellenangaben
Volume: 9,
Issue: 2,
Pages: 347-352
Publisher
American Chemical Society (ACS)
Publishing Place
Washington
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)