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Vesicular monoamine transporter
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====TBZ binding site==== TBZ and dihydrotetrabenazine (DTBZOH) are believed to bind to a different binding site from the RES/substrate binding site, or to a different conformation of the RES/substrate binding site.<ref name="Wimalasena, K. 2011"/><ref name="Chaudhry FA 2007"/><ref>{{cite journal |vauthors=Liu Y, Edwards RH | year = 1997 | title = The role of vesicular transport proteins in synaptic transmission and neural degeneration | journal = Annu. Rev. Neurosci. | volume = 20 | pages = 125β156 | doi=10.1146/annurev.neuro.20.1.125| pmid = 9056710 }}</ref> This site is believed to be located at the [[N-terminus]], based on studies done in bovine VMAT2.<ref name="Chaudhry FA 2007"/> Tyr434 and asp461 are identified as being responsible for the high-affinity interaction of TBZ, serotonin, and histamine in VMAT2.<ref name="Chaudhry FA 2007"/> Unlike methamphetamine, amphetamine binds to the TBZ site on hVMAT2.<ref name="VMAT2 amph vs meth">{{cite journal |vauthors=Sulzer D, Sonders MS, Poulsen NW, Galli A |title=Mechanisms of neurotransmitter release by amphetamines: a review |journal=Prog. Neurobiol. |volume=75 |issue=6 |pages=406β433 |date=April 2005 |pmid=15955613 |doi=10.1016/j.pneurobio.2005.04.003 |s2cid=2359509 |quote=They also demonstrated competition for binding between METH and reserpine, suggesting they might bind to the same site on VMAT. George Uhl's laboratory similarly reported that AMPH displaced the VMAT2 blocker tetrabenazine (Gonzalez et al., 1994)....tetrabenazine and reserpine are thought to bind to different sites on VMAT (Schuldiner et al., 1993a)}}</ref> Unlike RES inhibition, TBZ inhibition is only affected by very high concentrations of monoamines; however, single injections of RES can inhibit TBZ binding.<ref name="Chaudhry FA 2007"/> [[ketanserin]] (KET)<ref name="Wimalasena, K. 2011"/><ref name = "Darchen"/> and [[lobeline]]<ref name="Wimalasena, K. 2011"/><ref name="Chaudhry FA 2007"/> also bind to the TBZ binding site conformation.
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