The AXH domain adopts alternative folds: The solution structure of HBP1 AXH

Structure

Volumn 13, Issue 5, 2005, Pages 743-753

  De Chiara, Cesira ^a   Menon, Rajesh P ^a   Adinolfi, Salvatore ^a   De Boer, Jasper ^a   Ktistaki, Eleni ^a   Kelly, Geoff ^a   Calder, Lesley ^a   Kioussis, Dimitris ^a   Pastore, Annalisa ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MONOMER; NUCLEIC ACID; PROTEIN; PROTEIN AXH; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR HBP 1; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; FIBER; GENE MUTATION; INTERMETHOD COMPARISON; PATHOGENESIS; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STATISTICAL SIGNIFICANCE;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; HIGH MOBILITY GROUP PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; RNA; RNA-BINDING PROTEINS; SEQUENCE ALIGNMENT; SOLUTIONS; SPINOCEREBELLAR ATAXIAS;

ATAXIA;

EID: 18944394158     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.02.016     Document Type: Article

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