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Tripeptide binding in a proton‐dependent oligopeptide transporter

Martinez Molledo, Maria ; Quistgaard, Esben M. ; Löw, Christian

FEBS letters, 2018-10, Vol.592 (19), p.3239-3247 [Periódico revisado por pares]

England: John Wiley and Sons Inc

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Citações Citado por
  • Título:
    Tripeptide binding in a proton‐dependent oligopeptide transporter
  • Autor: Martinez Molledo, Maria ; Quistgaard, Esben M. ; Löw, Christian
  • Assuntos: Communication ; major facilitator superfamily (MFS) ; Medicin och hälsovetenskap ; membrane protein crystallography ; peptide binding ; peptide transporters ; POTs
  • É parte de: FEBS letters, 2018-10, Vol.592 (19), p.3239-3247
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
    Maria Martinez Molledo and Esben M. Quistgaard contributed equally to this article.
    Edited by Stuart Ferguson
  • Descrição: Proton‐dependent oligopeptide transporters (POTs) 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 thermophilus (PepTSt). We furthermore determined a 2.3‐Å structure of PepTSt 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.
  • Editor: England: John Wiley and Sons Inc
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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