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Check out this exciting new opportunity to join the cell pharmacology / cell screening group at Genesis Therapeutics!!! Check out this job from…
Check out this exciting new opportunity to join the cell pharmacology / cell screening group at Genesis Therapeutics!!! Check out this job from…
Liked by Evan Feinberg
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Excited to share the news of our collaboration with Gilead!
Excited to share the news of our collaboration with Gilead!
Shared by Evan Feinberg
Experience & Education
Publications
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Structural insights into µ-opioid receptor activation
Nature
From the abstract, "Activation of the μ-opioid receptor (μOR) is responsible for the efficacy of the most effective analgesics. To shed light on the structural basis for μOR activation, here we report a 2.1 Å X-ray crystal structure of the murine μOR bound to the morphinan agonist BU72 and a G protein mimetic camelid antibody fragment. The BU72-stabilized changes in the μOR binding pocket are subtle and differ from those observed for agonist-bound structures of the β2-adrenergic receptor (β2AR)…
From the abstract, "Activation of the μ-opioid receptor (μOR) is responsible for the efficacy of the most effective analgesics. To shed light on the structural basis for μOR activation, here we report a 2.1 Å X-ray crystal structure of the murine μOR bound to the morphinan agonist BU72 and a G protein mimetic camelid antibody fragment. The BU72-stabilized changes in the μOR binding pocket are subtle and differ from those observed for agonist-bound structures of the β2-adrenergic receptor (β2AR) and the M2 muscarinic receptor. Comparison with active β2AR reveals a common rearrangement in the packing of three conserved amino acids in the core of the μOR, and molecular dynamics simulations illustrate how the ligand-binding pocket is conformationally linked to this conserved triad. Additionally, an extensive polar network between the ligand-binding pocket and the cytoplasmic domains appears to play a similar role in signal propagation for all three G-protein-coupled receptors."
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Structural basis for chemokine recognition and activation of a viral G protein–coupled receptor
Science
From the absract, "Chemokines are small proteins that function as immune modulators through activation of chemokine G protein–coupled receptors (GPCRs). Several viruses also encode chemokines and chemokine receptors to subvert the host immune response. How protein ligands activate GPCRs remains unknown. We report the crystal structure at 2.9 angstrom resolution of the human cytomegalovirus GPCR US28 in complex with the chemokine domain of human CX3CL1 (fractalkine). The globular body of CX3CL1…
From the absract, "Chemokines are small proteins that function as immune modulators through activation of chemokine G protein–coupled receptors (GPCRs). Several viruses also encode chemokines and chemokine receptors to subvert the host immune response. How protein ligands activate GPCRs remains unknown. We report the crystal structure at 2.9 angstrom resolution of the human cytomegalovirus GPCR US28 in complex with the chemokine domain of human CX3CL1 (fractalkine). The globular body of CX3CL1 is perched on top of the US28 extracellular vestibule, whereas its amino terminus projects into the central core of US28. The transmembrane helices of US28 adopt an active-state–like conformation. Atomic-level simulations suggest that the agonist-independent activity of US28 may be due to an amino acid network evolved in the viral GPCR to destabilize the receptor’s inactive state."
Other authorsSee publication -
Synthesis, pharmacokinetics, and biological use of lysine-modified single-walled carbon nanotubes
International Journal of Nanomedicine
Patents
Honors & Awards
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Forbes 30 under 30
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https://www.forbes.com/30-under-30/2020/healthcare/
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Blue Waters Graduate Fellowship
National Center for Supercomputing Applications
Full funding for graduate school and extensive time on the Blue Waters supercomputer.
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The Applied Physics Prize
Yale University
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Phi Beta Kappa
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