The transmembrane tyrosines Y56, Y91 and Y167 play important roles in determining the affinity and transport rate of the rabbit proton-coupled peptide transporter PepT1
Open Access
- 30 November 2009
- journal article
- Published by Elsevier BV in The International Journal of Biochemistry & Cell Biology
- Vol. 41 (11), 2204-2213
- https://doi.org/10.1016/j.biocel.2009.04.014
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- A Cation–π Interaction between Extracellular TEA and an Aromatic Residue in Potassium ChannelsThe Journal of general physiology, 2006
- Molecular Modeling of PepT1 — Towards a StructureThe Journal of Membrane Biology, 2006
- Site-directed Mutation of Arginine 282 to Glutamate Uncouples the Movement of Peptides and Protons by the Rabbit Proton-peptide Cotransporter PepT1Journal of Biological Chemistry, 2004
- Analysis of Transmembrane Segment 7 of the Dipeptide Transporter hPepT1 by Cysteine-scanning MutagenesisPublished by Elsevier BV ,2003
- Structure and Mechanism of the Lactose Permease of Escherichia coliScience, 2003
- Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathwayBiochemical and Biophysical Research Communications, 2003
- How to Make Drugs Orally Active: A Substrate Template for Peptide Transporter PepT1Angewandte Chemie-International Edition, 2000
- Membrane Topology of the Human Dipeptide Transporter, hPEPT1, Determined by Epitope InsertionsBiochemistry, 1998
- Molecular identification of a role for tyrosine 167 in the function of the human intestinal proton- coupled dipeptide transporter (hPepT1).Biochemical and Biophysical Research Communications, 1998
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982