7PMX

HsPepT1 bound to Ala-Phe in the outward facing open conformation

7PMX の概要

• エントリーDOI: 10.2210/pdb7pmx/pdb
• EMDBエントリー: 13543
• 分子名称: Solute carrier family 15 member 1, ALA-PHE (2 entities in total)
• 機能のキーワード: hspept1, pept1, peptide transporter, membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79108.69

構造登録者

Killer, M.,Wald, J.,Pieprzyk, J.,Marlovits, T.C.,Loew, C. (登録日: 2021-09-03, 公開日: 2021-10-20, 最終更新日: 2024-07-17)

主引用文献

Killer, 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

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

実験手法

ELECTRON MICROSCOPY (3.5 Å)