Beta conformation of polyglutamine track revealed by a crystal structure of huntingtin N-terminal region with insertion of three histidine residues

Prion

Volumn 7, Issue 3, 2013, Pages 221-228

  Kim, Meewhi ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

strand; turn; Aggregation; Amyloid; Ataxia; Crystallography; Hairpin; Huntingtin; Polyglutamine; Prion

Indexed keywords

HISTIDINE; HUNTINGTIN; POLYGLUTAMINE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CRYSTAL STRUCTURE; CRYSTALLIZATION; EXON; HUNTINGTON DISEASE LIKE SYNDROME; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN INTERACTION;

Β-STRAND; Β-TURN; AMYLOID; CRYSTALLOGRAPHY; HAIRPIN; HUNTINGTIN; POLYGLUTAMINE; PRION; SGGREGATION; STAXIA;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 84879809556     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.23807     Document Type: Article

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