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• W2891540701 abstract "Proton‐dependent oligopeptide transporters ( POT s) are important for the uptake of di‐/tripeptides in many organisms and for drug transport in humans. The binding mode of dipeptides has been well described. However, it is still debated how tripeptides are recognized. Here, we show that tripeptides of the sequence Phe‐Ala‐Xxx bind with similar affinities as dipeptides to the POT transporter from Streptococcus thermophilu s (Pep T S t ). We furthermore determined a 2.3‐Å structure of Pep T S t in complex with Phe‐Ala‐Gln. The phenylalanine and alanine residues of the peptide adopt the same positions as previously observed for the Phe‐Ala dipeptide, while the glutamine side chain extends into a hitherto uncharacterized pocket. This pocket is adaptable in size and can likely accommodate a wide variety of peptide side chains." @default.
• W2891540701 created "2018-09-27" @default.
• W2891540701 creator A5033336724 @default.
• W2891540701 creator A5060449678 @default.
• W2891540701 creator A5087226390 @default.
• W2891540701 date "2018-09-21" @default.
• W2891540701 modified "2023-09-30" @default.
• W2891540701 title "Tripeptide binding in a proton‐dependent oligopeptide transporter" @default.
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• W2891540701 doi "https://doi.org/10.1002/1873-3468.13246" @default.
• W2891540701 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6221056" @default.
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• W2891540701 hasPublicationYear "2018" @default.
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