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Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors

Eph receptors are the largest family of receptor tyrosine kinases and by interactions with ephrin ligands mediate a myriad of processes from embryonic development to adult tissue homeostasis. The interaction of Eph receptors, especially at their transmembrane (TM) domains is key to understanding the...

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Detalles Bibliográficos
Autores principales: Sahoo, Amita R., Buck, Matthias
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8395321/
https://www.ncbi.nlm.nih.gov/pubmed/34445298
http://dx.doi.org/10.3390/ijms22168593
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author Sahoo, Amita R.
Buck, Matthias
author_facet Sahoo, Amita R.
Buck, Matthias
author_sort Sahoo, Amita R.
collection PubMed
description Eph receptors are the largest family of receptor tyrosine kinases and by interactions with ephrin ligands mediate a myriad of processes from embryonic development to adult tissue homeostasis. The interaction of Eph receptors, especially at their transmembrane (TM) domains is key to understanding their mechanism of signal transduction across cellular membranes. We review the structural and functional aspects of EphA1/A2 association and the techniques used to investigate their TM domains: NMR, molecular modelling/dynamics simulations and fluorescence. We also introduce transmembrane peptides, which can be used to alter Eph receptor signaling and we provide a perspective for future studies.
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spelling pubmed-83953212021-08-28 Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors Sahoo, Amita R. Buck, Matthias Int J Mol Sci Review Eph receptors are the largest family of receptor tyrosine kinases and by interactions with ephrin ligands mediate a myriad of processes from embryonic development to adult tissue homeostasis. The interaction of Eph receptors, especially at their transmembrane (TM) domains is key to understanding their mechanism of signal transduction across cellular membranes. We review the structural and functional aspects of EphA1/A2 association and the techniques used to investigate their TM domains: NMR, molecular modelling/dynamics simulations and fluorescence. We also introduce transmembrane peptides, which can be used to alter Eph receptor signaling and we provide a perspective for future studies. MDPI 2021-08-10 /pmc/articles/PMC8395321/ /pubmed/34445298 http://dx.doi.org/10.3390/ijms22168593 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Sahoo, Amita R.
Buck, Matthias
Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
title Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
title_full Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
title_fullStr Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
title_full_unstemmed Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
title_short Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
title_sort structural and functional insights into the transmembrane domain association of eph receptors
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8395321/
https://www.ncbi.nlm.nih.gov/pubmed/34445298
http://dx.doi.org/10.3390/ijms22168593
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