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