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Paramagnetic ligand tagging to identify protein binding sites

Journal article
Authors Ulrika Brath
S.I. Swami
Alberte X. Veiga
C.C. Tung
F. Van Petegem
Mate Erdelyi
Published in Journal of the American Chemical Society
Volume 137
Issue 35
Pages 11391-11398
ISSN 0002-7863
Publication year 2015
Published at Swedish NMR Centre at Göteborg University
Department of Chemistry and Molecular Biology
Pages 11391-11398
Language en
Keywords paramagnetic, NMR, calmodulin, sevoflurane
Subject categories Chemical Sciences, Organic Chemistry, Physical organic chemistry, Chemistry


Transient biomolecular interactions are the cornerstones of the cellular machinery. The identification of the binding sites for low affinity molecular encounters is essential for the development of high affinity pharmaceuticals from weakly binding leads but is hindered by the lack of robust methodologies for characterization of weakly binding complexes. We introduce a paramagnetic ligand tagging approach that enables localization of low affinity protein–ligand binding clefts by detection and analysis of intermolecular protein NMR pseudocontact shifts, which are invoked by the covalent attachment of a paramagnetic lanthanoid chelating tag to the ligand of interest. The methodology is corroborated by identification of the low millimolar volatile anesthetic interaction site of the calcium sensor protein calmodulin. It presents an efficient route to binding site localization for low affinity complexes and is applicable to rapid screening of protein–ligand systems with varying binding affinity.

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