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Esben Meldgaard Høgh Quistgaard

Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. / Guettou, Fatma; Quistgaard, Esben M; Raba, Michael; Moberg, Per; Löw, Christian; Nordlund, Pär.

In: Nature Structural and Molecular Biology, Vol. 21, No. 8, 08.2014, p. 728-31.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Guettou, F, Quistgaard, EM, Raba, M, Moberg, P, Löw, C & Nordlund, P 2014, 'Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2', Nature Structural and Molecular Biology, vol. 21, no. 8, pp. 728-31. https://doi.org/10.1038/nsmb.2860

APA

Guettou, F., Quistgaard, E. M., Raba, M., Moberg, P., Löw, C., & Nordlund, P. (2014). Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. Nature Structural and Molecular Biology, 21(8), 728-31. https://doi.org/10.1038/nsmb.2860

CBE

Guettou F, Quistgaard EM, Raba M, Moberg P, Löw C, Nordlund P. 2014. Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. Nature Structural and Molecular Biology. 21(8):728-31. https://doi.org/10.1038/nsmb.2860

MLA

Vancouver

Guettou F, Quistgaard EM, Raba M, Moberg P, Löw C, Nordlund P. Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. Nature Structural and Molecular Biology. 2014 Aug;21(8):728-31. https://doi.org/10.1038/nsmb.2860

Author

Guettou, Fatma ; Quistgaard, Esben M ; Raba, Michael ; Moberg, Per ; Löw, Christian ; Nordlund, Pär. / Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. In: Nature Structural and Molecular Biology. 2014 ; Vol. 21, No. 8. pp. 728-31.

Bibtex

@article{edc12f241f3543d99a420eefa245ff41,
title = "Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2",
abstract = "Peptide transporters of the PepT family have key roles in the transport of di- and tripeptides across membranes as well as in the absorption of orally administered drugs in the small intestine. We have determined structures of a PepT transporter from Shewanella oneidensis (PepT(So2)) in complex with three different peptides. The peptides bind in a large cavity lined by residues that are highly conserved in human PepT1 and PepT2. The bound peptides adopt extended conformations with their N termini clamped into a conserved polar pocket. A positively charged patch allows differential interactions with the C-terminal carboxylates of di- and tripeptides. Here we identify three pockets for peptide side chain interactions, and our binding studies define differential roles of these pockets for the recognition of different subtypes of peptide side chains.",
keywords = "Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Humans, Hydrophobic and Hydrophilic Interactions, Kinetics, Models, Molecular, Shewanella, Structural Homology, Protein, Substrate Specificity, Symporters, Journal Article, Research Support, Non-U.S. Gov't",
author = "Fatma Guettou and Quistgaard, {Esben M} and Michael Raba and Per Moberg and Christian L{\"o}w and P{\"a}r Nordlund",
year = "2014",
month = aug,
doi = "10.1038/nsmb.2860",
language = "English",
volume = "21",
pages = "728--31",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "8",

}

RIS

TY - JOUR

T1 - Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2

AU - Guettou, Fatma

AU - Quistgaard, Esben M

AU - Raba, Michael

AU - Moberg, Per

AU - Löw, Christian

AU - Nordlund, Pär

PY - 2014/8

Y1 - 2014/8

N2 - Peptide transporters of the PepT family have key roles in the transport of di- and tripeptides across membranes as well as in the absorption of orally administered drugs in the small intestine. We have determined structures of a PepT transporter from Shewanella oneidensis (PepT(So2)) in complex with three different peptides. The peptides bind in a large cavity lined by residues that are highly conserved in human PepT1 and PepT2. The bound peptides adopt extended conformations with their N termini clamped into a conserved polar pocket. A positively charged patch allows differential interactions with the C-terminal carboxylates of di- and tripeptides. Here we identify three pockets for peptide side chain interactions, and our binding studies define differential roles of these pockets for the recognition of different subtypes of peptide side chains.

AB - Peptide transporters of the PepT family have key roles in the transport of di- and tripeptides across membranes as well as in the absorption of orally administered drugs in the small intestine. We have determined structures of a PepT transporter from Shewanella oneidensis (PepT(So2)) in complex with three different peptides. The peptides bind in a large cavity lined by residues that are highly conserved in human PepT1 and PepT2. The bound peptides adopt extended conformations with their N termini clamped into a conserved polar pocket. A positively charged patch allows differential interactions with the C-terminal carboxylates of di- and tripeptides. Here we identify three pockets for peptide side chain interactions, and our binding studies define differential roles of these pockets for the recognition of different subtypes of peptide side chains.

KW - Bacterial Proteins

KW - Binding Sites

KW - Crystallography, X-Ray

KW - Humans

KW - Hydrophobic and Hydrophilic Interactions

KW - Kinetics

KW - Models, Molecular

KW - Shewanella

KW - Structural Homology, Protein

KW - Substrate Specificity

KW - Symporters

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/nsmb.2860

DO - 10.1038/nsmb.2860

M3 - Journal article

C2 - 25064511

VL - 21

SP - 728

EP - 731

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 8

ER -