TMalphaDB and TMbetaDB

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...

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Detalles Bibliográficos
Autores: Perea, Marc, Lugtenburg, Ivar, Mayol, Eduardo|||0000-0003-3120-8667, Cordomí Montoya, Arnau|||0000-0002-3848-2928, Deupi, Xavier|||0000-0003-4572-9316, Pardo Carrasco, Leonardo|||0000-0003-1778-7420, Olivella, Mireia|||0000-0002-6035-3399
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:254427
Acceso en línea:https://ddd.uab.cat/record/254427
https://dx.doi.org/urn:doi:10.1186/s12859-015-0699-5
Access Level:acceso abierto
Palabra clave:Membrane proteins
Transmembrane segments
Sequence motifs
Structural distortion
Descripción
Sumario: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. We have developed two web servers-TMalphaDB for α-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 side chain torsion angle, unit bend and unit twist. 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/TMalphaDB and http://lmc.uab.cat/TMbetaDB.