Abstract
Background Neurotransmitter:sodium symporters (NSS) are integral membrane proteins that mediate the reuptake of monoamine neurotransmitters previously released into the synaptic cleft. They are of pharmacological significance because they are the target of many clinically important drugs. LeuTAa, a leucine/alanine transporter is a bacterial homolog to NSS. Crystal structures of LeuTAa with open to outward, occluded and inward-facing states have already been resolved at high resolution. Hence, LeuTAa serves as a good paradigm for exploring the structurefunction relationship of NSS proteins.
Highlights
Neurotransmitter:sodium symporters (NSS) are integral membrane proteins that mediate the reuptake of monoamine neurotransmitters previously released into the synaptic cleft
lanthanide-based resonance energy transfer (LRET)-based measurements require the introduction of an LBT to accommodate terbium as the donor element and fluorophores chemically linked to a cysteine residue as the acceptor element
LBT tags and cysteine are introduced at selected positions in LeuTAa
Summary
Decrypting structural and functional changes in LeuTAa at atomic level employing LRET.
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