The SWIB and the MDM2 domains are homologous and share a common fold

Bioinformatics. 2002 Apr;18(4):626-30. doi: 10.1093/bioinformatics/18.4.626.

Abstract

Using a novel algorithm for protein sequence/structure analysis, we propose a probable homology between the SWIB domain (the conserved domain of the 60 kda subunit of the SWIB complex involved in chromatin remodelling) and the p53-binding domain of the MDM2 oncoprotein. The homology suggests that the SWIB domain would adopt a structure similar to that of the MDM2 domain and that these two families of proteins may share a similar functional mechanism.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms*
  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / genetics
  • Chlamydia / genetics
  • Chromosomal Proteins, Non-Histone / chemistry*
  • Chromosomal Proteins, Non-Histone / genetics*
  • Databases, Protein
  • Genes, p53 / genetics
  • Genome, Bacterial
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • National Library of Medicine (U.S.)
  • Nuclear Proteins*
  • Protein Conformation
  • Protein Folding
  • Proto-Oncogene Proteins / chemistry*
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogene Proteins c-mdm2
  • Sequence Alignment / methods*
  • Sequence Homology
  • Transcription Factors / chemistry*
  • Transcription Factors / genetics*
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / genetics
  • United States

Substances

  • Bacterial Outer Membrane Proteins
  • Chromosomal Proteins, Non-Histone
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • SWI-SNF-B chromatin-remodeling complex
  • Transcription Factors
  • Tumor Suppressor Protein p53
  • protein 60K, Chlamydia trachomatis
  • MDM2 protein, human
  • Proto-Oncogene Proteins c-mdm2