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MENSAdb: a thorough structural analysis of membrane protein dimers

Membrane proteins (MPs) are key players in a variety of different cellular processes and constitute the target of around 60% of all Food and Drug Administration–approved drugs. Despite their importance, there is still a massive lack of relevant structural, biochemical and mechanistic information mai...

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Autores principales: Matos-Filipe, Pedro, Preto, António J, Koukos, Panagiotis I, Mourão, Joana, Bonvin, Alexandre M J J, Moreira, Irina S
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8023553/
https://www.ncbi.nlm.nih.gov/pubmed/33822911
http://dx.doi.org/10.1093/database/baab013
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author Matos-Filipe, Pedro
Preto, António J
Koukos, Panagiotis I
Mourão, Joana
Bonvin, Alexandre M J J
Moreira, Irina S
author_facet Matos-Filipe, Pedro
Preto, António J
Koukos, Panagiotis I
Mourão, Joana
Bonvin, Alexandre M J J
Moreira, Irina S
author_sort Matos-Filipe, Pedro
collection PubMed
description Membrane proteins (MPs) are key players in a variety of different cellular processes and constitute the target of around 60% of all Food and Drug Administration–approved drugs. Despite their importance, there is still a massive lack of relevant structural, biochemical and mechanistic information mainly due to their localization within the lipid bilayer. To help fulfil this gap, we developed the MEmbrane protein dimer Novel Structure Analyser database (MENSAdb). This interactive web application summarizes the evolutionary and physicochemical properties of dimeric MPs to expand the available knowledge on the fundamental principles underlying their formation. Currently, MENSAdb contains features of 167 unique MPs (63% homo- and 37% heterodimers) and brings insights into the conservation of residues, accessible solvent area descriptors, average B-factors, intermolecular contacts at 2.5 Å and 4.0 Å distance cut-offs, hydrophobic contacts, hydrogen bonds, salt bridges, π–π stacking, T-stacking and cation–π interactions. The regular update and organization of all these data into a unique platform will allow a broad community of researchers to collect and analyse a large number of features efficiently, thus facilitating their use in the development of prediction models associated with MPs. Database URL: http://www.moreiralab.com/resources/mensadb.
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spelling pubmed-80235532021-04-09 MENSAdb: a thorough structural analysis of membrane protein dimers Matos-Filipe, Pedro Preto, António J Koukos, Panagiotis I Mourão, Joana Bonvin, Alexandre M J J Moreira, Irina S Database (Oxford) Database Tool Membrane proteins (MPs) are key players in a variety of different cellular processes and constitute the target of around 60% of all Food and Drug Administration–approved drugs. Despite their importance, there is still a massive lack of relevant structural, biochemical and mechanistic information mainly due to their localization within the lipid bilayer. To help fulfil this gap, we developed the MEmbrane protein dimer Novel Structure Analyser database (MENSAdb). This interactive web application summarizes the evolutionary and physicochemical properties of dimeric MPs to expand the available knowledge on the fundamental principles underlying their formation. Currently, MENSAdb contains features of 167 unique MPs (63% homo- and 37% heterodimers) and brings insights into the conservation of residues, accessible solvent area descriptors, average B-factors, intermolecular contacts at 2.5 Å and 4.0 Å distance cut-offs, hydrophobic contacts, hydrogen bonds, salt bridges, π–π stacking, T-stacking and cation–π interactions. The regular update and organization of all these data into a unique platform will allow a broad community of researchers to collect and analyse a large number of features efficiently, thus facilitating their use in the development of prediction models associated with MPs. Database URL: http://www.moreiralab.com/resources/mensadb. Oxford University Press 2021-04-05 /pmc/articles/PMC8023553/ /pubmed/33822911 http://dx.doi.org/10.1093/database/baab013 Text en © The Author(s) 2021. Published by Oxford University Press. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Database Tool
Matos-Filipe, Pedro
Preto, António J
Koukos, Panagiotis I
Mourão, Joana
Bonvin, Alexandre M J J
Moreira, Irina S
MENSAdb: a thorough structural analysis of membrane protein dimers
title MENSAdb: a thorough structural analysis of membrane protein dimers
title_full MENSAdb: a thorough structural analysis of membrane protein dimers
title_fullStr MENSAdb: a thorough structural analysis of membrane protein dimers
title_full_unstemmed MENSAdb: a thorough structural analysis of membrane protein dimers
title_short MENSAdb: a thorough structural analysis of membrane protein dimers
title_sort mensadb: a thorough structural analysis of membrane protein dimers
topic Database Tool
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8023553/
https://www.ncbi.nlm.nih.gov/pubmed/33822911
http://dx.doi.org/10.1093/database/baab013
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