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7PN1

Apo HsPepT1 in the outward facing open conformation

Summary for 7PN1
Entry DOI10.2210/pdb7pn1/pdb
EMDB information13545
DescriptorSolute carrier family 15 member 1 (1 entity in total)
Functional Keywordshspept1, pept1, peptide transporter, membrane protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight78872.42
Authors
Killer, M.,Wald, J.,Pieprzyk, J.,Marlovits, T.C.,Loew, C. (deposition date: 2021-09-04, release date: 2021-10-20, Last modification date: 2024-07-17)
Primary citationKiller, M.,Wald, J.,Pieprzyk, J.,Marlovits, T.C.,Low, C.
Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes.
Sci Adv, 7:eabk3259-eabk3259, 2021
Cited by
PubMed Abstract: The uptake of peptides in mammals plays a crucial role in nutrition and inflammatory diseases. This process is mediated by promiscuous transporters of the solute carrier family 15, which form part of the major facilitator superfamily. Besides the uptake of short peptides, peptide transporter 1 (PepT1) is a highly abundant drug transporter in the intestine and represents a major route for oral drug delivery. PepT2 also allows renal drug reabsorption from ultrafiltration and brain-to-blood efflux of neurotoxic compounds. Here, we present cryogenic electron microscopy (cryo-EM) structures of human PepT1 and PepT2 captured in four different states throughout the transport cycle. The structures reveal the architecture of human peptide transporters and provide mechanistic insights into substrate recognition and conformational transitions during transport. This may support future drug design efforts to increase the bioavailability of different drugs in the human body.
PubMed: 34730990
DOI: 10.1126/sciadv.abk3259
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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