TMalphaDB and TMbetaDB: Web servers to study the structural role of sequence motifs in aα-helix and β-barrel domains of membrane proteins

Marc Perea, Ivar Lugtenburg, Eduardo Mayol, Arnau Cordomí, Xavier Deupí, Leonardo Pardo, Mireia Olivella

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

© 2015 Perea et al. Background: Membrane proteins represent over 25% of human protein genes and account for more than 60% of drug targets due to their accessibility from the extracellular environment. The increasing number of available crystal structures of these proteins in the Protein Data Bank permits an initial estimation of their structural properties. Description: We have developed two web servers-TMalphaDB for aα-helix bundles and TMbetaDB for β-barrels-to analyse the growing repertoire of available crystal structures of membrane proteins. TMalphaDB and TMbetaDB permit to search for these specific sequence motifs in a non-redundant structure database of transmembrane segments and quantify structural parameters such as ϕ and Ψ backbone dihedral angles, Χ<inf>1</inf> side chain torsion angle, unit bend and unit twist. Conclusions: The structural information offered by TMalphaDB and TMbetaDB permits to quantify structural distortions induced by specific sequence motifs, and to elucidate their role in the 3D structure. This specific structural information has direct implications in homology modeling of the growing sequences of membrane proteins lacking experimental structure. TMalphaDB and TMbetaDB are freely available at http://lmc.uab.cat/TMalphaDBand http://lmc.uab.cat/TMbetaDB .
Original languageEnglish
Article number266
JournalBMC Bioinformatics
Volume16
Issue number1
DOIs
Publication statusPublished - 20 Aug 2015

Keywords

  • Membrane proteins
  • Sequence motifs
  • Structural distortion
  • Transmembrane segments

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