title: Atomistic models of ion and solute transport by the sodium-dependent secondary active transporters.
abstract: The recent determination of high-resolution crystal structures of several transporters offers unprecedented insights into the structural mechanisms behind secondary transport. These proteins utilize the facilitated diffusion of the ions down their electrochemical gradients to transport the substrate against its concentration gradient. The structural studies revealed striking similarities in the structural organization of ion and solute binding sites and a well-conserved inverted-repeat topology between proteins from several gene families. In this paper we will overview recent atomistic simulations applied to study the mechanisms of selective binding of ion and substrate in LeuT, Glt, vSGLT and hSERT as well as its consequences for the transporter conformational dynamics. This article is part of a Special Issue entitled: Membrane protein structure and function.
authors.affiliation: Institute for Biocomplexity and Informatics (IBI), University of Calgary, 2500 University Drive, Calgary, Canada, T2N 1N4.
authors.forename: Igor
authors.initials: I
authors.lastname: Zdravkovic
authors.forename: Chunfeng
authors.initials: C
authors.lastname: Zhao
authors.forename: Bogdan
authors.initials: B
authors.lastname: Lev
authors.forename: Javier Eduardo
authors.initials: JE
authors.lastname: Cuervo
authors.forename: Sergei Yu
authors.initials: SY
authors.lastname: Noskov
mesh_terms: D000818:Animals; D001665:Binding Sites; D001692:Biological Transport; D006801:Humans; D007477:Ions / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D012964:Sodium / Q000378:metabolism*
chemical_list: D007477:Ions; D026901:Membrane Transport Proteins; D012964:Sodium