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

Assignment of IVL-Methyl side chain of the ligand-free monomeric human MALT1 paracaspase-IgL3 domain in solution

Autor: Xiao Han, Maria Levkovets, Dmitry Lesovoy, Renhua Sun, Johan Wallerstein, Tatyana Sandalova, Tatiana Agback, Adnane Achour, Peter Agback, Vladislav Yu. Orekhov

Publikováno v: Biomolecular NMR Assignments. 16:363-371

Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these path

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1889b3e36845f001c4609951166c2679
https://doi.org/10.1007/s12104-022-10105-3

Entropy–Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C

Autor: Esko Oksanen, Majda Misini Ignjatović, Ulrika Brath, Octav Caldararu, Sven Wernersson, Kristoffer Peterson, Derek T. Logan, Ulf J. Nilsson, Ulf Ryde, Vilhelm Ekberg, Johan Wallerstein, Mikael Akke, Rohit Kumar, Hakon Leffler

Publikováno v: JACS Au
JACS Au 1(4), 484-500 (2021). doi:10.1021/jacsau.0c00094
JACS Au, Vol 1, Iss 4, Pp 484-500 (2021)

JACS Au 1(4), 484-500 (2021). doi:10.1021/jacsau.0c00094
Molecular recognition is fundamental to biological signaling. A central question is how individual interactions between molecular moieties affect the thermodynamics of ligand binding to pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f862f31eae11a8c886b7c8019ca91b21
https://doi.org/10.1021/jacsau.0c00094

Elucidation of hydrogen bonding patterns in ligand-free, lactose- and glycerol-bound galectin-3C by neutron crystallography to guide drug design

Autor: Matthew P. Blakeley, Leighton Coates, Johan Wallerstein, Derek T. Logan, Francesco Manzoni, Mikael Akke, Andreas Ostermann, Esko Oksanen, Tobias E. Schrader

Publikováno v: 'Journal of Medicinal Chemistry ', vol: 61, pages: 4412-4420 (2018)
Journal of medicinal chemistry 61(10), 4412-4420 (2018). doi:10.1021/acs.jmedchem.8b00081

The medically important drug target galectin-3 binds galactose-containing moieties on glycoproteins through an intricate pattern of hydrogen bonds to a largely polar surface-exposed binding site. All successful inhibitors of galectin-3 to date have b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d1a385d53dcde50893fe5338748110c
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ILL:27486