Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a consid...

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Detalles Bibliográficos
Autores principales: Delaforge, Elise, Milles, Sigrid, Huang, Jie-rong, Bouvier, Denis, Jensen, Malene Ringkjøbing, Sattler, Michael, Hart, Darren J., Blackledge, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2016
Materias:
Molecular Biosciences
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5020063/
https://www.ncbi.nlm.nih.gov/pubmed/27679800
http://dx.doi.org/10.3389/fmolb.2016.00054
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author Delaforge, Elise
Milles, Sigrid
Huang, Jie-rong
Bouvier, Denis
Jensen, Malene Ringkjøbing
Sattler, Michael
Hart, Darren J.
Blackledge, Martin
author_facet Delaforge, Elise
Milles, Sigrid
Huang, Jie-rong
Bouvier, Denis
Jensen, Malene Ringkjøbing
Sattler, Michael
Hart, Darren J.
Blackledge, Martin
author_sort Delaforge, Elise
collection PubMed
description Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.
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spelling pubmed-50200632016-09-27 Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions Delaforge, Elise Milles, Sigrid Huang, Jie-rong Bouvier, Denis Jensen, Malene Ringkjøbing Sattler, Michael Hart, Darren J. Blackledge, Martin Front Mol Biosci Molecular Biosciences Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales. Frontiers Media S.A. 2016-09-13 /pmc/articles/PMC5020063/ /pubmed/27679800 http://dx.doi.org/10.3389/fmolb.2016.00054 Text en Copyright © 2016 Delaforge, Milles, Huang, Bouvier, Jensen, Sattler, Hart and Blackledge. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Delaforge, Elise
Milles, Sigrid
Huang, Jie-rong
Bouvier, Denis
Jensen, Malene Ringkjøbing
Sattler, Michael
Hart, Darren J.
Blackledge, Martin
Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
title Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
title_full Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
title_fullStr Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
title_full_unstemmed Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
title_short Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
title_sort investigating the role of large-scale domain dynamics in protein-protein interactions
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5020063/
https://www.ncbi.nlm.nih.gov/pubmed/27679800
http://dx.doi.org/10.3389/fmolb.2016.00054
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