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|Title:||Structural insights into substrate recognition in proton-dependent oligopeptide transporters||Authors:||Quistgaard, Esben M.
Jong, Agnes Jin Oi
|Issue Date:||2013||Source:||Guettou, F., Quistgaard, E. M., Trésaugues, L., Moberg, P., Jegerschöld, C., Zhu, L., Jong, A. J. O., Nordlund, P.,& Löw, C. (2013). Structural insights into substrate recognition in proton-dependent oligopeptide transporters. EMBO reports,14(9), 749-845.||Series/Report no.:||EMBO reports||Abstract:||Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)—a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs.||URI:||https://hdl.handle.net/10356/99088
|DOI:||10.1038/embor.2013.107||Rights:||© 2013 EUROPEAN MOLECULAR BIOLOGY ORGANIZATION. This paper was published in EMBO reports and is made available as an electronic reprint (preprint) with permission of EUROPEAN MOLECULAR BIOLOGY ORGANIZATION. The paper can be found at the following official DOI: http://dx.doi.org/10.1038/embor.2013.107. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
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