MeMotif: a database of linear motifs in alpha-helical transmembrane proteins

Publikation: Beitrag in FachzeitschriftForschungsartikelBeigetragenBegutachtung

Beitragende

  • Annalisa Marsico - , Biotechnologisches Zentrum (BIOTEC) (Autor:in)
  • Kerstin Scheubert - (Autor:in)
  • Anne Tuukkanen - (Autor:in)
  • Andreas Henschel - (Autor:in)
  • Christof Winter - (Autor:in)
  • Rainer Winnenburg - (Autor:in)
  • Michael Schroeder - , Professur für Bioinformatik (Autor:in)

Abstract

Membrane proteins are important for many processes in the cell and used as main drug targets. The increasing number of high-resolution structures available makes for the first time a characterization of local structural and functional motifs in alpha-helical transmembrane proteins possible. MeMotif (http://projects.biotec.tu-dresden.de/memotif) is a database and wiki which collects more than 2000 known and novel computationally predicted linear motifs in alpha-helical transmembrane proteins. Motifs are fully described in terms of several structural and functional features and editable. Motifs contained in MeMotif can be used in different biological applications, from the identification of biochemically important functional residues which are candidates for mutagenesis experiments to the improvement of tools for transmembrane protein modeling.

Details

OriginalspracheEnglisch
Seiten (von - bis)D181-9
FachzeitschriftNucleic acids research
Jahrgang38
AusgabenummerIssue suool_1
PublikationsstatusVeröffentlicht - Jan. 2010
Peer-Review-StatusJa

Externe IDs

PubMedCentral PMC2808916
Scopus 75549084896
ORCID /0000-0003-2848-6949/work/141543388

Schlagworte

Schlagwörter

  • Amino Acid Motifs, Bacterial Proteins/chemistry, Computational Biology/methods, Databases, Genetic, Databases, Nucleic Acid, Databases, Protein, Information Storage and Retrieval/methods, Internet, Membrane Proteins/chemistry, Protein Structure, Secondary, Protein Structure, Tertiary, Software

Bibliotheksschlagworte