10.1371/journal.pcbi.1004578.g004
Silvia Lovera
Silvia
Lovera
Maria Morando
Maria
Morando
Encarna Pucheta-Martinez
Encarna
Pucheta-Martinez
Jorge L. Martinez-Torrecuadrada
Jorge L.
Martinez-Torrecuadrada
Giorgio Saladino
Giorgio
Saladino
Francesco L. Gervasio
Francesco L.
Gervasio
Free energy of the A-loop opening.
Public Library of Science
2015
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 03:24:58
Figure
https://plos.figshare.com/articles/figure/_Free_energy_of_the_A_loop_opening_/1612622
<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>