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Title: MENSAdb: a thorough structural analysis of membrane protein dimers
Authors: Matos-Filipe, Pedro 
Preto, Antonio J. 
Koukos, Panagiotis I. 
Mourão, Joana 
Bonvin, Alexandre M. J. J. 
Moreira, Irina S. 
Issue Date: 5-Apr-2021
Publisher: Oxford University Press
Project: POCI-01-0145-FEDER-031356 
Serial title, monograph or event: Database
Volume: 2021
Abstract: 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.
ISSN: 1758-0463
DOI: 10.1093/database/baab013
Rights: openAccess
Appears in Collections:I&D CNC - Artigos em Revistas Internacionais
IIIUC - Artigos em Revistas Internacionais
FCTUC Ciências da Vida - Artigos em Revistas Internacionais
I&D CIBB - Artigos em Revistas Internacionais

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