Journal article
Crystal structures of the extracellular domain from PepT1 and PepT2 provide novel insights into mammalian peptide transport
- Abstract:
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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 ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 2.7MB, Terms of use)
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- Publisher copy:
- 10.1016/j.str.2015.07.016
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Funding
Bibliographic Details
- Publisher:
- Cell Press
- Journal:
- Structure (London, England : 1993) More from this journal
- Volume:
- 23
- Issue:
- 10
- Pages:
- 1889-1899
- Publication date:
- 2015-10-01
- DOI:
- EISSN:
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1878-4186
- ISSN:
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0969-2126
Item Description
- Language:
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English
- Pubs id:
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pubs:541671
- UUID:
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uuid:5c7327d0-dd12-4499-a5fe-8fca60a5aa2a
- Local pid:
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pubs:541671
- Source identifiers:
-
541671
- Deposit date:
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2015-11-12
Terms of use
- Copyright holder:
- Beale et al
- Copyright date:
- 2015
- Notes:
- Copyright © 2015 The Authors. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- Licence:
- CC Attribution (CC BY)
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