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ECD of PepT1 interacts with TM1 to facilitate substrate transport
Open accessPreprint — published as 10.1016/j.str.2022.04.011 · Paper page
Abstract
Mammalian peptide transporters, PepT1 and PepT2, mediate uptake of a wide variety of di- and tri-peptides and are essential for the absorption of dietary peptides in the digestive tract and the recovery of peptides in renal filtrate. PepT also mediates absorption of many drugs and prodrugs to enhance their bioavailability. PepT has 12 transmembrane (TM) helices that fold into two domains, the N-terminal domain (NTD, TM1-6) and C-terminal domain (CTD, TM7-12), and a large extracellular domain (ECD) of ∼200 amino acids between TM9 and TM10. It is known that peptide transport involves large motions of the N- and C-domains, but the role of ECD remains unclear. Here we report the structure of PepT1 from Equus caballus (horse) determined by cryo-electron microscopy. The structure shows that ECD interacts with TM1 and bridges the N- and C-domains. Deletion of the ECD or mutations to the TM1-ECD interface both impair the transport activity. These results demonstrate a role of ECD in structure and function of PepT1 and enhance our understanding of the mechanism of transport in PepT1.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Shen, J., Hu, M., Ren, Z., Fan, X., Portioli, C., Yan, X., Rong, M., & Zhou, M.
- Affiliations
- Baylor College of Medicine (US)
- Princeton University (US)
- Corresponding author
- Fan, Xiao
- Zhou, Ming
- Venue
- Structure
- Publisher
- openRxiv
- Published
- 2022-03-02
- Volume
- 30
- Issue
- 7
- Pages
- 1035-1041.e3
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC10404463
- OpenAlex
- W4280558405
- Cited by
- 29
- References
- 1
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 14 · 2023: 4 · 2022: 2
- FWCI
- 2.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Structure (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Commons-TMC (Texas Medical Center) (submittedVersion)
- Funders
- National Science Foundation (1420541)
- Cancer Prevention and Research Institute of Texas (R1223)
- Princeton Center for Complex Materials (DMR-1420541)
- National Institutes of Health (HL086392)
- Materials Research Science and Engineering Center, Harvard University (DMR 1420541, 1420541)
- National Heart, Lung, and Blood Institute (R01HL086392)
- National Institute of General Medical Sciences (R01GM098878, RM1GM145416)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK122784)
- Division of Materials Research (DMR- 1420541, 1420541)
- Topics
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- PepT1, peptide transporters, extracellular domain, transmembrane helices, peptide absorption, drug absorption, apo conformation, lipid nanodiscs, transporter structure, transport mechanisms, horses
- MeSH terms
- Peptide Transporter 1, Animals, Biological Transport, Horses, Mammals, Molecular Conformation, Peptides, Symporters
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