Sandbox: Difference between revisions
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contributes significantly to drug-drug interactions and drug disposition. However, the structural basis of specific | contributes significantly to drug-drug interactions and drug disposition. However, the structural basis of specific | ||
substrate and inhibitor transport by human OAT1 (hOAT1) has remained elusive. Here are four | substrate and inhibitor transport by human OAT1 (hOAT1) has remained elusive. Here are four | ||
cryogenic electron microscopy | [[cryogenic electron microscopy]] (cryo-EM) structures of hOAT1 in its inward-facing conformation: the apo | ||
form, the substrate (olmesartan)-bound form with different anions, and the inhibitor (probenecid)-bound | form, the substrate (olmesartan)-bound form with different anions, and the inhibitor (probenecid)-bound | ||
form. | form. | ||
