TY - JOUR
T1 - MENSAdb
T2 - a thorough structural analysis of membrane protein dimers
AU - Matos-Filipe, Pedro
AU - Preto, António J
AU - Koukos, Panagiotis I
AU - Mourão, Joana
AU - Bonvin, Alexandre M J J
AU - Moreira, Irina S
N1 - Funding Information:
A.J.P. was also supported by FCT through PhD scholarship SFRH/BD/144966/2019. I.S.M. was funded by the FCT Investigator programme-IF/00578/2014 (co-financed by the European Social Fund and Programa Operacional Potencial Humano). A.M.J. and P.I.K acknowledge funding from the Dutch Foundation for Scientific Research (NWO) (TOP-PUNT grant 718.015.001). The authors would also like to acknowledge ERNEST (European Research Network on Signal Transduction, CA18133) and STRATAGEM (New diagnostic and therapeutic tools against multidrug-resistant tumours, CA17104).
Publisher Copyright:
© 2020 The Author(s). Published by Oxford University Press.
PY - 2021/4/5
Y1 - 2021/4/5
N2 - 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.
AB - 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.
U2 - 10.1093/database/baab013
DO - 10.1093/database/baab013
M3 - Article
C2 - 33822911
SN - 1758-0463
VL - 2021
JO - Database : the journal of biological databases and curation
JF - Database : the journal of biological databases and curation
M1 - baab013
ER -