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Prediction of GABARAP interaction with the GABA type A receptor

We have performed docking simulations on GABARAP interacting with the GABA type A receptor using SwarmDock. We have also used a novel method to study hydration sites on the surface of these two proteins; this method identifies regions around proteins where desolvation is relatively easy, and these a...

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Detalles Bibliográficos
Autores principales: Irwin, B.W.J., Vukovič, Siniša, Payne, M.C., ElGamacy, Mohammad, Chau, P.‐L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6492159/
https://www.ncbi.nlm.nih.gov/pubmed/30218455
http://dx.doi.org/10.1002/prot.25589
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author Irwin, B.W.J.
Vukovič, Siniša
Payne, M.C.
ElGamacy, Mohammad
Chau, P.‐L.
author_facet Irwin, B.W.J.
Vukovič, Siniša
Payne, M.C.
ElGamacy, Mohammad
Chau, P.‐L.
author_sort Irwin, B.W.J.
collection PubMed
description We have performed docking simulations on GABARAP interacting with the GABA type A receptor using SwarmDock. We have also used a novel method to study hydration sites on the surface of these two proteins; this method identifies regions around proteins where desolvation is relatively easy, and these are possible locations where proteins can bind each other. There is a high degree of consistency between the predictions of these two methods. Moreover, we have also identified binding sites on GABARAP for other proteins, and listed possible binding sites for as yet unknown proteins on both GABARAP and the GABA type A receptor intracellular domain.
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spelling pubmed-64921592019-05-06 Prediction of GABARAP interaction with the GABA type A receptor Irwin, B.W.J. Vukovič, Siniša Payne, M.C. ElGamacy, Mohammad Chau, P.‐L. Proteins Research Articles We have performed docking simulations on GABARAP interacting with the GABA type A receptor using SwarmDock. We have also used a novel method to study hydration sites on the surface of these two proteins; this method identifies regions around proteins where desolvation is relatively easy, and these are possible locations where proteins can bind each other. There is a high degree of consistency between the predictions of these two methods. Moreover, we have also identified binding sites on GABARAP for other proteins, and listed possible binding sites for as yet unknown proteins on both GABARAP and the GABA type A receptor intracellular domain. John Wiley & Sons, Inc. 2018-11-04 2018-12 /pmc/articles/PMC6492159/ /pubmed/30218455 http://dx.doi.org/10.1002/prot.25589 Text en © 2018 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals, Inc. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Irwin, B.W.J.
Vukovič, Siniša
Payne, M.C.
ElGamacy, Mohammad
Chau, P.‐L.
Prediction of GABARAP interaction with the GABA type A receptor
title Prediction of GABARAP interaction with the GABA type A receptor
title_full Prediction of GABARAP interaction with the GABA type A receptor
title_fullStr Prediction of GABARAP interaction with the GABA type A receptor
title_full_unstemmed Prediction of GABARAP interaction with the GABA type A receptor
title_short Prediction of GABARAP interaction with the GABA type A receptor
title_sort prediction of gabarap interaction with the gaba type a receptor
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6492159/
https://www.ncbi.nlm.nih.gov/pubmed/30218455
http://dx.doi.org/10.1002/prot.25589
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