Protein dynamics and conformational selection in bidirectional signal transduction

Protein conformational dynamics simultaneously allow promiscuity and specificity in binding. The multiple conformations of the free EphA4 ligand-binding domain observed in two new EphA4 crystal structures provide a unique insight into the conformational dynamics of EphA4 and its signaling pathways....

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Detalles Bibliográficos
Autores principales: Nussinov, Ruth, Ma, Buyong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Commentary
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3266202/
https://www.ncbi.nlm.nih.gov/pubmed/22277130
http://dx.doi.org/10.1186/1741-7007-10-2
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author Nussinov, Ruth
Ma, Buyong
author_facet Nussinov, Ruth
Ma, Buyong
author_sort Nussinov, Ruth
collection PubMed
description Protein conformational dynamics simultaneously allow promiscuity and specificity in binding. The multiple conformations of the free EphA4 ligand-binding domain observed in two new EphA4 crystal structures provide a unique insight into the conformational dynamics of EphA4 and its signaling pathways. The heterogeneous ensemble and loop dynamics explain how the EphA4 receptor is able to bind multiple A- and B-ephrin ligands and small molecules via conformational selection, which helps to fine-tune cellular signal response in both receptor and ligand cells. See research article http://www.biomedcentral.com/2046-1682/5/2
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spelling pubmed-32662022012-01-26 Protein dynamics and conformational selection in bidirectional signal transduction Nussinov, Ruth Ma, Buyong BMC Biol Commentary Protein conformational dynamics simultaneously allow promiscuity and specificity in binding. The multiple conformations of the free EphA4 ligand-binding domain observed in two new EphA4 crystal structures provide a unique insight into the conformational dynamics of EphA4 and its signaling pathways. The heterogeneous ensemble and loop dynamics explain how the EphA4 receptor is able to bind multiple A- and B-ephrin ligands and small molecules via conformational selection, which helps to fine-tune cellular signal response in both receptor and ligand cells. See research article http://www.biomedcentral.com/2046-1682/5/2 BioMed Central 2012-01-25 /pmc/articles/PMC3266202/ /pubmed/22277130 http://dx.doi.org/10.1186/1741-7007-10-2 Text en Copyright ©2012 Nussinov and Ma; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Commentary
Nussinov, Ruth
Ma, Buyong
Protein dynamics and conformational selection in bidirectional signal transduction
title Protein dynamics and conformational selection in bidirectional signal transduction
title_full Protein dynamics and conformational selection in bidirectional signal transduction
title_fullStr Protein dynamics and conformational selection in bidirectional signal transduction
title_full_unstemmed Protein dynamics and conformational selection in bidirectional signal transduction
title_short Protein dynamics and conformational selection in bidirectional signal transduction
title_sort protein dynamics and conformational selection in bidirectional signal transduction
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3266202/
https://www.ncbi.nlm.nih.gov/pubmed/22277130
http://dx.doi.org/10.1186/1741-7007-10-2
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