Repeat-swap homology modeling of secondary active transporters: updated protocol and prediction of elevator-type mechanisms.

ABSTRACT: Secondary active transporters are critical for neurotransmitter clearance and recycling during synaptic transmission and uptake of nutrients. These proteins mediate the movement of solutes against their concentration gradients, by using the energy released in the movement of ions down pre-existing concentration gradients. To achieve this, transporters conform to the so-called alternating-access hypothesis, whereby the protein adopts at least two conformations in which the substrate binding sites are exposed to one or other side of the membrane, but not both simultaneously. Structures of a bacterial homolog of neuronal glutamate transporters, GltPh, in several different conformational states have revealed that the protein structure is asymmetric in the outward- and inward-open states, and t

SUBMITTER: Vergara-Jaque A 

PROVIDER: S-EPMC4560100 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature