Conformational Stability and Substrate Translocation - A Computational Study of the Leucine Transporter

Abstract

a calmodulin regulation site that with many disease mutations reside proximately. using a variety of spectroscopic methods including CD, fluorescence, NMR, we have determined metal binding affinity, stoichiometry, conformational change and binding modes of Ca 2þ and Calmodulin.

Characterization of Lipid–Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation

“…347 The study showed that the hydrophobic mismatch is different in distinct conformations (outward-open, occluded, inward-open) of LeuT, and that the differences are connected to the structural elements involved in the conformational transitions during the transport cycle. 347,348 Beyond hydrophobic-hydrophilic contacts between the membrane and the embedded protein, specific lipids can regulate the dynamics and conformational transitions of the LeuT-fold NSSs upon direct interactions. Microsecond AA simulations of human dopamine transporter (hDAT) in a PIP 2 -enriched membrane revealed an inward opening of the transporter triggered by PIP 2 -mediated electrostatic association of specific structural motifs.…”