Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.

Using a combination of genomic and post-genomic approaches is rapidly altering the number of identified human influx carriers. A transmembrane protein bilitranslocase (TCDB 2.A.65) has long attracted attention because of its function as an organic anion carrier. It has also been identified as a pote...

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Autores principales:	Andrej Perdih, Amrita Roy Choudhury, Špela Župerl, Emilia Sikorska, Igor Zhukov, Tom Solmajer, Marjana Novič
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/aa8ba365b16943e6934c67c91b00aadd
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spelling	oai:doaj.org-article:aa8ba365b16943e6934c67c91b00aadd2021-11-18T07:14:53ZStructural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.1932-620310.1371/journal.pone.0038967https://doaj.org/article/aa8ba365b16943e6934c67c91b00aadd2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22745694/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Using a combination of genomic and post-genomic approaches is rapidly altering the number of identified human influx carriers. A transmembrane protein bilitranslocase (TCDB 2.A.65) has long attracted attention because of its function as an organic anion carrier. It has also been identified as a potential membrane transporter for cellular uptake of several drugs and due to its implication in drug uptake, it is extremely important to advance the knowledge about its structure. However, at present, only the primary structure of bilitranslocase is known. In our work, transmembrane subunits of bilitranslocase were predicted by a previously developed chemometrics model and the stability of these polypeptide chains were studied by molecular dynamics (MD) simulation. Furthermore, sodium dodecyl sulfate (SDS) micelles were used as a model of cell membrane and herein we present a high-resolution 3D structure of an 18 amino acid residues long peptide corresponding to the third transmembrane part of bilitranslocase obtained by use of multidimensional NMR spectroscopy. It has been experimentally confirmed that one of the transmembrane segments of bilitranslocase has alpha helical structure with hydrophilic amino acid residues oriented towards one side, thus capable of forming a channel in the membrane.Andrej PerdihAmrita Roy ChoudhuryŠpela ŽuperlEmilia SikorskaIgor ZhukovTom SolmajerMarjana NovičPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 6, p e38967 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Andrej Perdih Amrita Roy Choudhury Špela Župerl Emilia Sikorska Igor Zhukov Tom Solmajer Marjana Novič Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.
description	Using a combination of genomic and post-genomic approaches is rapidly altering the number of identified human influx carriers. A transmembrane protein bilitranslocase (TCDB 2.A.65) has long attracted attention because of its function as an organic anion carrier. It has also been identified as a potential membrane transporter for cellular uptake of several drugs and due to its implication in drug uptake, it is extremely important to advance the knowledge about its structure. However, at present, only the primary structure of bilitranslocase is known. In our work, transmembrane subunits of bilitranslocase were predicted by a previously developed chemometrics model and the stability of these polypeptide chains were studied by molecular dynamics (MD) simulation. Furthermore, sodium dodecyl sulfate (SDS) micelles were used as a model of cell membrane and herein we present a high-resolution 3D structure of an 18 amino acid residues long peptide corresponding to the third transmembrane part of bilitranslocase obtained by use of multidimensional NMR spectroscopy. It has been experimentally confirmed that one of the transmembrane segments of bilitranslocase has alpha helical structure with hydrophilic amino acid residues oriented towards one side, thus capable of forming a channel in the membrane.
format	article
author	Andrej Perdih Amrita Roy Choudhury Špela Župerl Emilia Sikorska Igor Zhukov Tom Solmajer Marjana Novič
author_facet	Andrej Perdih Amrita Roy Choudhury Špela Župerl Emilia Sikorska Igor Zhukov Tom Solmajer Marjana Novič
author_sort	Andrej Perdih
title	Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.
title_short	Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.
title_full	Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.
title_fullStr	Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.
title_full_unstemmed	Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.
title_sort	structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/aa8ba365b16943e6934c67c91b00aadd
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Structural analysis of a peptide fragment of transmembrane transporter protein bilitranslocase.

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