The NMR solution structure of AIM2 PYD domain from Mus musculus reveals a distinct α2-α3 helix conformation from its human homologues

Biochemical and Biophysical Research Communications

Volumn 461, Issue 2, 2015, Pages 396-400

  Hou, Xianhui ^a,b   Niu, Xiaogang ^a,b  

^a PEKING UNIVERSITY   (China)

^b PEKING UNIVERSITY   (China)

Author keywords

AIM2; Inflammasome; NMR; PYD; Self association; Solution structure

Indexed keywords

AIM2 PROTEIN, HUMAN; AIM2 PROTEIN, MOUSE; DNA BINDING PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; MOLECULAR GENETICS; MOUSE; NUCLEAR MAGNETIC RESONANCE; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMALS; DNA-BINDING PROTEINS; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

EID: 84937759923     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.04.046     Document Type: Article

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