Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19

PEX19 is a chaperone and import receptor for peroxisomal membrane proteins (PMPs). Here the authors present the structure of the farnesylated C-terminal domain of PEX19, and its interaction with PMPs reveals how the farnesyl moiety allosterically reshapes the PMP binding surface and modulates PEX19...

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Autores principales: Leonidas Emmanouilidis, Ulrike Schütz, Konstantinos Tripsianes, Tobias Madl, Juliane Radke, Robert Rucktäschel, Matthias Wilmanns, Wolfgang Schliebs, Ralf Erdmann, Michael Sattler
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Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/b5af4d4e62a8425b95894fbe959afdf2
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spelling oai:doaj.org-article:b5af4d4e62a8425b95894fbe959afdf22021-12-02T14:42:33ZAllosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX1910.1038/ncomms146352041-1723https://doaj.org/article/b5af4d4e62a8425b95894fbe959afdf22017-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms14635https://doaj.org/toc/2041-1723PEX19 is a chaperone and import receptor for peroxisomal membrane proteins (PMPs). Here the authors present the structure of the farnesylated C-terminal domain of PEX19, and its interaction with PMPs reveals how the farnesyl moiety allosterically reshapes the PMP binding surface and modulates PEX19 function.Leonidas EmmanouilidisUlrike SchützKonstantinos TripsianesTobias MadlJuliane RadkeRobert RucktäschelMatthias WilmannsWolfgang SchliebsRalf ErdmannMichael SattlerNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Leonidas Emmanouilidis
Ulrike Schütz
Konstantinos Tripsianes
Tobias Madl
Juliane Radke
Robert Rucktäschel
Matthias Wilmanns
Wolfgang Schliebs
Ralf Erdmann
Michael Sattler
Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19
description PEX19 is a chaperone and import receptor for peroxisomal membrane proteins (PMPs). Here the authors present the structure of the farnesylated C-terminal domain of PEX19, and its interaction with PMPs reveals how the farnesyl moiety allosterically reshapes the PMP binding surface and modulates PEX19 function.
format article
author Leonidas Emmanouilidis
Ulrike Schütz
Konstantinos Tripsianes
Tobias Madl
Juliane Radke
Robert Rucktäschel
Matthias Wilmanns
Wolfgang Schliebs
Ralf Erdmann
Michael Sattler
author_facet Leonidas Emmanouilidis
Ulrike Schütz
Konstantinos Tripsianes
Tobias Madl
Juliane Radke
Robert Rucktäschel
Matthias Wilmanns
Wolfgang Schliebs
Ralf Erdmann
Michael Sattler
author_sort Leonidas Emmanouilidis
title Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19
title_short Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19
title_full Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19
title_fullStr Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19
title_full_unstemmed Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19
title_sort allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor pex19
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/b5af4d4e62a8425b95894fbe959afdf2
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