Membrane Proteins (MPs) account for around 15-39% of the human proteome and assume a critical role in a vast set of cellular and physiological mechanisms, including molecular transport, nutrient uptake, toxin and waste product clearance, respiration, and signaling. While roughly 60% of all FDA-approved drugs target MPs, there is a shortage of structural and biochemical data on them mainly hindered by their localization in the lipid bilayer. We present here MEmbrane protein dimer Novel Structure Analyser database (MENSAdb), a real time web-application exposing a broad array of fundamental features about MPs surface and their interfacial regions. In particular, we present conservation, four distinctive Accessible Solvent Area (ASA) descriptors, average and environment-specific B-factors, intermolecular contacts at 2.5 and 4.0 angstroms distance cutoffs, salt-bridges, hydrogen-bonds, hydrophobic, pi-pi interactions, t-stacking and cation-pi interactions. Additionally, users can closely inspect differences in values between three distinctive residues classes: i) non-surface, ii) surface and non-interfacial and iii) interfacial. The database is freely available at www.moreiralab.com/resources/mensadb.
@article{arxiv.1902.02321,
title = {MENSADB: A Thorough Structural Analysis of Membrane Protein Dimers},
author = {Pedro Matos-Filipe and António J. Preto and Panagiotis I. Koukos and Joana Mourão and Alexandre M. J. J. Bonvin and Irina S. Moreira},
journal= {arXiv preprint arXiv:1902.02321},
year = {2019}
}