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A versatile structural domain analysis server using profile weight matrices.

Steffen Schmidt1, Peer Bork, Thomas Dandekar

  • 1EMBL, Postfach 102209, D-69012 Heidelberg, Germany.

Journal of Chemical Information and Computer Sciences
|March 26, 2002
PubMed
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The AnDom web tool identifies structural protein domains within sequences, aiding structural genomics and the study of complex protein families. It offers fast predictions for large and multidomain proteins.

Area of Science:

  • Structural biology
  • Bioinformatics
  • Genomics

Background:

  • Identifying structural domains in protein sequences is crucial for understanding protein function and evolution.
  • Existing methods may struggle with large or multidomain proteins, limiting their application in structural genomics.

Purpose of the Study:

  • To develop and present AnDom, a web tool for assigning experimentally determined structural domains to protein sequences.
  • To provide a fast and efficient method for domain assignment applicable to complex protein families.

Main Methods:

  • Utilizes profile-specific matrices derived from custom multiple sequence alignments of SCOP (Structural Classification of Proteins) domains (version 1.50).
  • Employs a web server for user-friendly access and domain prediction.

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Main Results:

  • AnDom accurately assigns structural domains to protein sequences, including those of multidomain and large proteins.
  • The prediction process is computationally efficient, offering short prediction times.

Conclusions:

  • AnDom is a valuable resource for structural genomics, enabling rapid domain identification.
  • The tool facilitates the investigation of complex eukaryotic protein families and aids in protein structure prediction.