The HIN domain of IFI-200 proteins consists of two OB folds.
The interferon-inducible p200 (IFI-200/HIN-200) family of proteins regulates cell growth and differentiation, and confers resistance to the development of tumors and virus infections. IFI-200 family members are thought to exert their biological effects by modulation of the transcriptional activities of numerous factors and interaction with other proteins through the C-terminal HIN domains. However, the HIN domain structure and function have remained obscure. Therefore, we performed a comprehensive bioinformatics analysis and assembled a structure-based multiple sequence alignment of IFI-200 proteins. The application of fold recognition methods revealed that the HIN domain consists of two consecutive OB domains. Our structural models of DNA-binding HIN domains afford the long-sought interpretations for many previous experimental observations. Our results also raise the possibility of as yet unexplored functional roles of IFI-200 proteins as transcriptional regulators and as interaction partners of proteins involved in immunomodulatory and apoptotic processes.
Albrecht
Mario
M
Max-Planck-Institute for Informatics, Stuhlsatzenhausweg 85, 66123 Saarbrücken, Germany. mario.albrecht@mpi-sb.mpg.de
Choubey
Divaker
D
Lengauer
Thomas
T
D017209:Apoptosis; D001483:Base Sequence; D002454:Cell Differentiation / Q000502:physiology; D049109:Cell Proliferation; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry* / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology*; D016415:Sequence Alignment; D014158:Transcription, Genetic / Q000235:genetics / Q000502:physiology
D004268:DNA-Binding Proteins; C101635:HIN-200 protein, human; D009687:Nuclear Proteins