Article
Mechanism for alternating access in neurotransmitter transporters.
Proceedings of the National Academy of Sciences of the United States of America - 29 Jul 2008
Forrest Lucy R, Zhang Yuan-Wei, Jacobs Miriam T, Gesmonde Joan, Xie Li, Honig Barry H, Rudnick Gary
Abstract excerpt
Crystal structures of LeuT, a bacterial homologue of mammalian neurotransmitter transporters, show a molecule of bound substrate that is essentially exposed to the extracellular space but occluded from the cytoplasm. Thus, there must exist an alternate conformation for LeuT in which the substrate is accessible to the cytoplasm and a corresponding mechanism that switches accessibility from one side of the membrane...
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