Lovera, Silvia Morando, Maria Pucheta-Martinez, Encarna Martinez-Torrecuadrada, Jorge L. Saladino, Giorgio Gervasio, Francesco L. Free energy of the A-loop opening. <p>Free energy surfaces of Abl, Src, and drug-resistant mutants projected on the optimal path describing the conformational change of the A-loop from open to closed in Src (CV1) and Abl (CV2). The free energy minima corresponding to an extended A-loop active-like conformation are labeled “A”, “B” is used for A-loop semi-closed (inactive) conformations and “C” for fully closed A-loop conformations. The contour lines are drawn every 1 kcal/mol.</p> binding kinetics;mutation;imatinib resistance;Kinase Conformational Dynamics;T 315I gatekeeper;Drug Resistance;cancer patients;tyrosine kinases;ABL kinase domain;dynamics simulations;Myeloid leukemia;microcalorimetry experiments;DFG motif;energy calculations;binding mechanism;energy landscape 2015-11-25
    https://plos.figshare.com/articles/figure/_Free_energy_of_the_A_loop_opening_/1612622
10.1371/journal.pcbi.1004578.g004