PTR2/POT/NPF transporters: what makes them tick?

Publikation: Bidrag til tidsskriftReviewForskningfagfællebedømt

Standard

PTR2/POT/NPF transporters : what makes them tick? / Prabhala, Bala K.; Rahman, Moazur; Nour-Eldin, Hussam H; Jørgensen, Flemming Steen; Mirza, Osman.

I: Advances in Protein Chemistry and Structural Biology, Bind 123, 2021, s. 219-240.

Publikation: Bidrag til tidsskriftReviewForskningfagfællebedømt

Harvard

Prabhala, BK, Rahman, M, Nour-Eldin, HH, Jørgensen, FS & Mirza, O 2021, 'PTR2/POT/NPF transporters: what makes them tick?', Advances in Protein Chemistry and Structural Biology, bind 123, s. 219-240. https://doi.org/10.1016/bs.apcsb.2020.10.002

APA

Prabhala, B. K., Rahman, M., Nour-Eldin, H. H., Jørgensen, F. S., & Mirza, O. (2021). PTR2/POT/NPF transporters: what makes them tick? Advances in Protein Chemistry and Structural Biology, 123, 219-240. https://doi.org/10.1016/bs.apcsb.2020.10.002

Vancouver

Prabhala BK, Rahman M, Nour-Eldin HH, Jørgensen FS, Mirza O. PTR2/POT/NPF transporters: what makes them tick? Advances in Protein Chemistry and Structural Biology. 2021;123:219-240. https://doi.org/10.1016/bs.apcsb.2020.10.002

Author

Prabhala, Bala K. ; Rahman, Moazur ; Nour-Eldin, Hussam H ; Jørgensen, Flemming Steen ; Mirza, Osman. / PTR2/POT/NPF transporters : what makes them tick?. I: Advances in Protein Chemistry and Structural Biology. 2021 ; Bind 123. s. 219-240.

Bibtex

@article{25908b98e8b149cd84974e368b52aebf,
title = "PTR2/POT/NPF transporters: what makes them tick?",
abstract = "PTR2/POT/NPF are a family of primarily proton coupled transporters that belong to the major facilitator super family and are found across most kingdoms of life. They are involved in uptake of nutrients, hormones, ions and several orally administered drug molecules. A wealth of structural and functional data is available for this family; the similarity between the protein structural features have been discussed and investigated in detail on several occasions, however there are no reports on the unification of substrate information. In order to fill this gap, we have collected information about substrates across the entire PTR2/POT/NPF family in order to provide key insights into what makes a molecule a substrate and whether there are common features among confirmed substrates. This review will be of particular interest for researchers in the field trying to probe the mechanisms responsible for the different selectivity of these transporters at a molecular resolution, and to design novel substrates.",
keywords = "Animals, Biological Transport, Humans, Membrane Transport Proteins/chemistry, Substrate Specificity",
author = "Prabhala, {Bala K.} and Moazur Rahman and Nour-Eldin, {Hussam H} and J{\o}rgensen, {Flemming Steen} and Osman Mirza",
note = "Copyright {\textcopyright} 2021 Elsevier Inc. All rights reserved.",
year = "2021",
doi = "10.1016/bs.apcsb.2020.10.002",
language = "English",
volume = "123",
pages = "219--240",
journal = "Advances in Protein Chemistry and Structural Biology",
issn = "1876-1623",
publisher = "Academic Press",

}

RIS

TY - JOUR

T1 - PTR2/POT/NPF transporters

T2 - what makes them tick?

AU - Prabhala, Bala K.

AU - Rahman, Moazur

AU - Nour-Eldin, Hussam H

AU - Jørgensen, Flemming Steen

AU - Mirza, Osman

N1 - Copyright © 2021 Elsevier Inc. All rights reserved.

PY - 2021

Y1 - 2021

N2 - PTR2/POT/NPF are a family of primarily proton coupled transporters that belong to the major facilitator super family and are found across most kingdoms of life. They are involved in uptake of nutrients, hormones, ions and several orally administered drug molecules. A wealth of structural and functional data is available for this family; the similarity between the protein structural features have been discussed and investigated in detail on several occasions, however there are no reports on the unification of substrate information. In order to fill this gap, we have collected information about substrates across the entire PTR2/POT/NPF family in order to provide key insights into what makes a molecule a substrate and whether there are common features among confirmed substrates. This review will be of particular interest for researchers in the field trying to probe the mechanisms responsible for the different selectivity of these transporters at a molecular resolution, and to design novel substrates.

AB - PTR2/POT/NPF are a family of primarily proton coupled transporters that belong to the major facilitator super family and are found across most kingdoms of life. They are involved in uptake of nutrients, hormones, ions and several orally administered drug molecules. A wealth of structural and functional data is available for this family; the similarity between the protein structural features have been discussed and investigated in detail on several occasions, however there are no reports on the unification of substrate information. In order to fill this gap, we have collected information about substrates across the entire PTR2/POT/NPF family in order to provide key insights into what makes a molecule a substrate and whether there are common features among confirmed substrates. This review will be of particular interest for researchers in the field trying to probe the mechanisms responsible for the different selectivity of these transporters at a molecular resolution, and to design novel substrates.

KW - Animals

KW - Biological Transport

KW - Humans

KW - Membrane Transport Proteins/chemistry

KW - Substrate Specificity

U2 - 10.1016/bs.apcsb.2020.10.002

DO - 10.1016/bs.apcsb.2020.10.002

M3 - Review

C2 - 33485485

VL - 123

SP - 219

EP - 240

JO - Advances in Protein Chemistry and Structural Biology

JF - Advances in Protein Chemistry and Structural Biology

SN - 1876-1623

ER -

ID: 272115649