The HIN domain of IFI-200 proteins consists of two OB folds

Biochemical and Biophysical Research Communications

Volumn 327, Issue 3, 2005, Pages 679-687

  Albrecht, Mario ^a   Choubey, Divaker ^b   Lengauer, Thomas ^a  

^a MAX PLANCK INSTITUTE FOR INFORMATICS   (Germany)

^b LOYOLA UNIVERSITY CHICAGO   (United States)

Author keywords

HIN 200; IFI 200; Interferon inducible; OB fold; pRb; Pyrin

Indexed keywords

INTERFERON INDUCIBLE PROTEIN P200; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; BINDING SITE; BIOINFORMATICS; IMMUNOMODULATION; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; TRANSCRIPTION REGULATION;

APOPTOSIS; BASE SEQUENCE; CELL DIFFERENTIATION; CELL PROLIFERATION; DNA-BINDING PROTEINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR PROTEINS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; TRANSCRIPTION, GENETIC;

EID: 11844278344     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.12.056     Document Type: Article

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