Role of Annular Lipids in the Functional Properties of Leucine Transporter LeuT Proteomicelles.

ABSTRACT: Recent work has shown that the choice of the type and concentration of detergent used for the solubilization of membrane proteins can strongly influence the results of functional experiments. In particular, the amino acid transporter LeuT can bind two substrate molecules in low concentrations of n-dodecyl β-d-maltopyranoside (DDM), whereas high concentrations reduce the molar binding stoichiometry to 1:1. Subsequent molecular dynamics (MD) simulations of LeuT in DDM proteomicelles revealed that DDM can penetrate to the extracellular vestibule and make stable contacts in the functionally important secondary substrate binding site (S2), suggesting a potential competitive mechanism for the reduction in binding stoichiometry. Because annular lipids can be retained during solubilization, we per

SUBMITTER: LeVine MV 

PROVIDER: S-EPMC4757857 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature