Interplay of halogen bonding and solvation in protein–ligand binding

Autor: Maria Luisa Verteramo, Majda Misini Ignjatović, Rohit Kumar, Sven Wernersson, Vilhelm Ekberg, Johan Wallerstein, Göran Carlström, Veronika Chadimová, Hakon Leffler, Fredrik Zetterberg, Derek T. Logan, Ulf Ryde, Mikael Akke, Ulf J. Nilsson

Publikováno v: iScience, Vol 27, Iss 4, Pp 109636- (2024)

Summary: Halogen bonding is increasingly utilized in efforts to achieve high affinity and selectivity of molecules designed to bind proteins, making it paramount to understand the relationship between structure, dynamics, and thermodynamic driving fo

Externí odkaz: https://doaj.org/article/04a7dad9b6fc435daabaaf102e239b88

Bromodomain Interactions with Acetylated Histone 4 Peptides in the BRD4 Tandem Domain: Effects on Domain Dynamics and Internal Flexibility

Autor: Sven Wernersson, Romel Bobby, Liz Flavell, Alexander G. Milbradt, Geoffrey A. Holdgate, Kevin J. Embrey, Mikael Akke

Publikováno v: Biochemistry. 61:2303-2318

The bromodomain and extra-terminal (BET) protein BRD4 regulates gene expression via recruitment of transcriptional regulatory complexes to acetylated chromatin. Like other BET proteins, BRD4 contains two bromodomains, BD1 and BD2, that can interact c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1248ad1f7c2a224824aa53c05db4b148
https://doi.org/10.1021/acs.biochem.2c00226

Backbone 1H, 13C, and 15N resonance assignments of BoMan26A, a β-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus

Autor: Cecilia Persson, Santosh Kumar Upadhyay, Viktoria Bågenholm, Henrik Stålbrand, Sven Wernersson, Mikael Akke

Publikováno v: Biomolecular Nmr Assignments

Bacteroides ovatus is a member of the human gut microbiota. The importance of this microbial consortium involves the degradation of complex dietary glycans mainly conferred by glycoside hydrolases. In this study we focus on one such catabolic glycosi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a7511e209015b286d5e34ebd76320aa
https://doi.org/10.1007/s12104-019-09879-w

Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity

Autor: Johan Härmark, Yoran Weide, Michal Respondek, Peter Højrup, Hans Hebert, Christopher A. G. Söderberg, Cecilia Emanuelsson, Mikael Akke, Gudrun Rutsdottir, Morten Rasmussen, Sven Wernersson, Philip J.B. Koeck

Publikováno v: The Journal of Biological Chemistry
Rutsdottir, G, Härmark, J, Weide, Y, Hebert, H, Rasmussen, M I, Wernersson, S, Respondek, M, Akke, M, Højrup, P, Koeck, P J B, Söderberg, C A G & Emanuelsson, C 2017, ' Structural model of dodecameric heat-shock protein Hsp21 : Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity ', Journal of Biological Chemistry, vol. 292, no. 19, pp. 8103-8121 . https://doi.org/10.1074/jbc.M116.766816

Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard to define due to limited structural informa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d51f096a2ad0dbc0aae919612d1ad62
https://pubmed.ncbi.nlm.nih.gov/28325834