Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes-Reference-Cited by-同舟云学术

Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes

Published:2021-11-05 Issue:45 Volume:7 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Killer Maxime¹²³^ORCID,Wald Jiri¹⁴⁵^ORCID,Pieprzyk Joanna¹²,Marlovits Thomas C.¹⁴⁵^ORCID,Löw Christian¹²^ORCID

Affiliation:

1. Centre for Structural Systems Biology (CSSB), Notkestrasse 85, D-22607 Hamburg, Germany.

2. European Molecular Biology Laboratory (EMBL), Hamburg Unit c/o Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, D-22607 Hamburg, Germany.

3. Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences, Faculty of Biosciences, Im Neuenheimer Feld 234, D-69120 Heidelberg, Germany.

4. Institute of Structural and Systems Biology, University Medical Center Hamburg-Eppendorf, Notkestrasse 85, D-22607 Hamburg, Germany.

5. Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, D-22607 Hamburg, Germany.

Abstract

Structures of PepT1 and PepT2 provide mechanistic insights into substrate and drug translocation across epithelial membranes.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference75 articles.

1. Evidence for two different modes of tripeptide disappearance in human intestine. Uptake by peptide carrier systems and hydrolysis by peptide hydrolases.

2. Analysis of the transport properties of side chain modified dipeptides at the mammalian peptide transporter PEPT1

3. Interaction of 31 β-lactam antibiotics with the H+/peptide symporter PEPT2: analysis of affinity constants and comparison with PEPT1

4. Differential Recognition of β-Lactam Antibiotics by Intestinal and Renal Peptide Transporters, PEPT 1 and PEPT 2

5. PEPT1 as a Paradigm for Membrane Carriers That Mediate Electrogenic Bidirectional Transport of Anionic, Cationic, and Neutral Substrates

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