7 Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, F-75005 Paris, France Sorbonne Universités, Université Pierre et Marie Curie, Université Paris 6, F-75005, Paris, France PMC article.6 Department of Chemistry, The University of Chicago, Chicago, IL 60637 Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637 James Franck Institute, The University of Chicago, Chicago, IL 60637 Computation Institute, The University of Chicago, Chicago, IL 60637.5 Chemical Biology of Membranes and Therapeutic Delivery Unit, Institut Curie, PSL Research University, CNRS UMR3666, INSERM U1143, F-75005 Paris, France.4 Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, F-75005 Paris, France.3 Laboratoire Charles Coulomb, UMR 5221 CNRS, Université de Montpellier, F-34095 Montpellier, France.1 Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, F-75005 Paris, France Department of Chemistry, The University of Chicago, Chicago, IL 60637 Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637 James Franck Institute, The University of Chicago, Chicago, IL 60637 Computation Institute, The University of Chicago, Chicago, IL 60637 2 Laboratory of Molecular Biology, Medical Research Council, Cambridge CB2 0QH, United Kingdom.Even more specifically, the invention relates to a functional fusion of a toxin and a scaffold protein wherein the folded scaffold protein interrupts the topology of the toxin by insertion in an exposed β-turn of a β-strand-containing domain of said toxin to form a rigid fusion protein that retains its high affinity target binding capacity. More specifically, the present invention relates to novel fusion proteins, their uses and methods in three-dimensional structural analysis of macromolecules, such as X-ray crystallography and high-resolution Cryo-EM, and their use in structure-based drug design and screening, and as pharmacological tools. Even more specifically, the invention relates to a functional fusion of a toxin and a scaffold protein wherein the folded scaffold protein interrupts the topology of the toxin by insertion in an exposed β-turn of a β-strand-containing domain of said toxin to form a rigid fusion protein that retains its high affinity target binding capacity.ĪB - The present invention relates to the field of structural biology and drug discovery.
N2 - The present invention relates to the field of structural biology and drug discovery. T1 - Fusion protein with a toxin and scaffold protein
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