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Reference: Beale, JH, Parker, JL, Samsudin, F et al., (2015). Crystal structures of the extracellular domain from PepT1 and PepT2 provide novel insights into mammalian peptide transport. Structure (London, England : 1993), 23 (10), 1889-1899.Citable link to this page:

 

Crystal structures of the extracellular domain from PepT1 and PepT2 provide novel insights into mammalian peptide transport

Abstract: Mammals obtain nitrogen via the uptake of di- and tri-peptides in the gastrointestinal tract through the action of PepT1 and PepT2, which are members of the POT family of proton-coupled oligopeptide transporters. PepT1 and PepT2 also play an important role in drug transport in the human body. Recent crystal structures of bacterial homologs revealed a conserved peptide-binding site and mechanism of transport. However, a key structural difference exists between bacterial and mammalian homologs with only the latter containing a large extracellular domain, the function of which is currently unknown. Here, we present the crystal structure of the extracellular domain from both PepT1 and PepT2 that reveal two immunoglobulin-like folds connected in tandem, providing structural insight into mammalian peptide transport. Functional and biophysical studies demonstrate that these domains interact with the intestinal protease trypsin, suggesting a role in clustering proteolytic activity to the site of peptide transport in eukaryotic cells.

Peer Review status:Peer reviewedPublication status:PublishedVersion:Publisher's version Funder: Medical Research Council   Funder: Wellcome Trust   Notes:Copyright © 2015 The Authors. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

Bibliographic Details

Publisher: Cell Press

Publisher Website: http://www.cell.com/

Journal: Structure (London, England : 1993)see more from them

Publication Website: http://www.structure.org/

Issue Date: 2015-10

pages:1889-1899Identifiers

Urn: uuid:5c7327d0-dd12-4499-a5fe-8fca60a5aa2a

Source identifier: 541671

Eissn: 1878-4186

Doi: https://doi.org/10.1016/j.str.2015.07.016

Issn: 0969-2126 Item Description

Type: Journal article;

Language: eng

Version: Publisher's version Tiny URL: pubs:541671

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Autor: Beale, JH - institutionUniversity of Oxford Oxford, MSD, Biochemistry - - - Parker, JL - institutionUniversity of Oxford Oxford,

Fuente: https://ora.ox.ac.uk/objects/uuid:5c7327d0-dd12-4499-a5fe-8fca60a5aa2a



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