title: MDAT- Aligning multiple domain arrangements.
abstract: BACKGROUND
  Proteins are composed of domains, protein segments that fold independently from the rest of the protein and have a specific function. During evolution the arrangement of domains can change: domains are gained, lost or their order is rearranged. To facilitate the analysis of these changes we propose the use of multiple domain alignments.
  
  
  RESULTS
  We developed an alignment program, called MDAT, which aligns multiple domain arrangements. MDAT extends earlier programs which perform pairwise alignments of domain arrangements. MDAT uses a domain similarity matrix to score domain pairs and aligns the domain arrangements using a consistency supported progressive alignment method.
  
  
  CONCLUSIONS
  MDAT will be useful for analysing changes in domain arrangements within and between protein families and will thus provide valuable insights into the evolution of proteins and their domains. MDAT is coded in C++, and the source code is freely available for download at http://www.bornberglab.org/pages/mdat .
authors: Institute for Evolution and Biodiversity, University of Münster, Hüfferstr. 1, Münster, Germany. c.kemena@uni-muenster.de.
authors: Carsten
authors: C
authors: Kemena
authors: Institute for Evolution and Biodiversity, University of Münster, Hüfferstr. 1, Münster, Germany. t.bitard.feildel@uni-muenster.de.
authors: Tristan
authors: T
authors: Bitard-Feildel
authors: Institute for Evolution and Biodiversity, University of Münster, Hüfferstr. 1, Münster, Germany. ebb@uni-muenster.de.
authors: Erich
authors: E
authors: Bornberg-Bauer
mesh_terms: D000465:Algorithms; D006801:Humans; D011381:Programming Languages; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*; D012984:Software
chemical_list: D011506:Proteins
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