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The Protein Mutant Database

T Kawabata1, M Ota, K Nishikawa

  • 1Center for Information Biology, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan. takawaba@lab.nig.ac.jp

Nucleic Acids Research
|December 10, 1998
PubMed
Summary
This summary is machine-generated.

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The protein mutant database (PMD) now includes over 81,000 mutants, accessible via a new integrated system. This system visualizes protein mutations and allows homology searches, enhancing protein research.

Area of Science:

  • Biochemistry
  • Bioinformatics
  • Structural Biology

Background:

  • The protein mutant database (PMD) curates extensive data on protein mutations from scientific literature.
  • Existing databases may lack integrated visualization and advanced retrieval functionalities for protein mutants.

Purpose of the Study:

  • To introduce a powerful new viewing and retrieving system for the protein mutant database (PMD).
  • To enhance accessibility and utility of protein mutant information for researchers.
  • To integrate protein sequence and tertiary structure data with mutation information.

Main Methods:

  • Development of a web-based system for accessing and visualizing protein mutant data.
  • Automatic generation of mutated protein sequences alongside wild-type sequences.

Related Experiment Videos

  • 3D structure visualization highlighting mutation sites for proteins with determined structures.
  • Implementation of sequence homology search functionality against the PMD.
  • Development of a feature to summarize mutations at specific sites across homologous proteins.

    • Main Results:

    • The PMD now contains over 81,000 mutants from approximately 10,000 articles.
    • The new system integrates sequence and tertiary structure data.
    • Mutated sequences are automatically generated and displayed with wild-type sequences, highlighting altered amino acids.
    • 3D structures visualize mutation sites.
    • Sequence homology searches and mutation summaries for homologous proteins are available.

    Conclusions:

    • The developed system significantly enhances the usability of the protein mutant database.
    • Researchers can now more effectively analyze and compare protein mutations.
    • The integrated approach facilitates a deeper understanding of protein structure-function relationships.