1. Lipids modulate the conformational dynamics of a secondary multidrug transporter.

    Nature Structural & Molecular Biology 23(8):744 (2016) PMID 27399258

    Direct interactions with lipids have emerged as key determinants of the folding, structure and function of membrane proteins, but an understanding of how lipids modulate protein dynamics is still lacking. Here, we systematically explored the effects of lipids on the conformational dynamics of th...
  2. Allosteric coupling from G protein to the agonist-binding pocket in GPCRs.

    Nature 535(7610):182 (2016) PMID 27362234

    G-protein-coupled receptors (GPCRs) remain the primary conduit by which cells detect environmental stimuli and communicate with each other. Upon activation by extracellular agonists, these seven-transmembrane-domain-containing receptors interact with heterotrimeric G proteins to regulate downstr...
  3. Allosteric regulation of G protein-coupled receptor activity by phospholipids.

    Nature Chemical Biology 12(1):35 (2016) PMID 26571351 PMCID PMC4718399

    Lipids are emerging as key regulators of membrane protein structure and activity. These effects can be attributed either to the modification of bilayer properties (thickness, curvature and surface tension) or to the binding of specific lipids to the protein surface. For G protein-coupled recepto...
  4. Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling

    Cell 162(6):1431 (2015)

  5. Structural Insights into the Dynamic Process of β2-Adrenergic Receptor Signaling.

    Cell 161(5):1101 (2015) PMID 25981665 PMCID PMC4441853

    G-protein-coupled receptors (GPCRs) transduce signals from the extracellular environment to intracellular proteins. To gain structural insight into the regulation of receptor cytoplasmic conformations by extracellular ligands during signaling, we examine the structural dynamics of the cytoplasmi...
  6. Protonation drives the conformational switch in the multidrug transporter LmrP.

    Nature Chemical Biology 10(2):149 (2014) PMID 24316739 PMCID PMC4749020

    Multidrug antiporters of the major facilitator superfamily couple proton translocation to the extrusion of cytotoxic molecules. The conformational changes that underlie the transport cycle and the structural basis of coupling of these transporters have not been elucidated. Here we used extensive...
  7. Studying the Conformational Cycle of the Secondary Multidrug Transporter LmrP by EPR Spectroscopy

    Biophysical Journal 102(3):660a (2012)

  8. Interactions between phosphatidylethanolamine headgroup and LmrP, a multidrug transporter: a conserved mechanism for proton gradient sensing?

    Journal of Biological Chemistry 283(14):9369 (2008) PMID 18234676

    In a number of cases, the function of membrane proteins appears to require the presence of specific lipid species in the bilayer. We have shown that the secondary multidrug transporter LmrP requires the presence of phosphatidylethanolamine (PE), as its replacement by phosphatidylcholine (PC) inh...
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