Constraints Imposed by the Membrane Selectively Guide the Alternating Access Dynamics of the Glutamate Transporter Glt(Ph)

Substrate transport in sodium-coupled amino acid symporters involves a large-scale conformational change that shifts the access to the substrate-binding site from one side of the membrane to the other. The structural change is particularly substantial and entails a unique piston-like quaternary rear...

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Bibliographic Details
Main Authors: Lezon, Timothy R., Bahar, Ivet
Format: Artigo
Language:Inglês
Published: The Biophysical Society 2012
Subjects:
Channels and Transporters
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3309413/
https://ncbi.nlm.nih.gov/pubmed/22455916
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2012.02.028
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