ArticleThe Journal of physiology2011
Residues R282 and D341 act as electrostatic gates in the proton-dependent oligopeptide transporter PepT1.
Article in The Journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- The teleost fish PepT1-type peptide transporters and their relationships with neutral and charged substrates.Frontiers in physiology · 2023Article
- The "www" ofMembranes · 2022Review
- Functional characterization of Atlantic salmon (Salmo salar L.) PepT2 transporters.The Journal of physiology · 2022Article
- Amino acid transporter B(0)AT1 (slc6a19) and ancillary protein: impact on function.Pflugers Archiv : European journal of physiology · 2016Article
- Conformational changes represent the rate-limiting step in the transport cycle of maize sucrose transporter1.The Plant cell · 2013Article
- Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1.Pflugers Archiv : European journal of physiology · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oligopeptide transporter PepT1 is a protein found in the membrane of the cells of the intestinal walls, and represents the main route through which proteic nutrients are absorbed by the organism. Along the polypeptidic chain of this protein, two oppositely charged amino acids, an arginine in position 282 and an aspartate in position 341 of the sequence, have been hypothesised to form a barrier in the absorption pathway. In this paper we show that appropriate mutations of these amino acids change the properties of PepT1 in a way that confirms that these parts of the protein indeed act as an electrostatic gate in the transport process. The identification of the structural basis of the functional mechanism of this transporter is important because, in addition to its role in nutrient uptake, PepT1 represents a major pathway for the absorption of several therapeutic drugs.
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Registered trials
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