Manipulation of reciprocal salt bridges at the heterodimerization interface alters the dimerization properties of mouse RXRα and PPARγ1

Biochemical and Biophysical Research Communications

Volumn 358, Issue 4, 2007, Pages 1080-1085

  Chan, Lap Shu ^a,b   Wells, Richard A ^a,b,c  

^a Institute of Clinical Evaluative Sciences   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c DEPARTMENT OF RADIATION ONCOLOGY   (Canada)

Author keywords

Charge reversal mutation; DNA binding domain; Electrophoretic mobility shift assay; HNF4; Ligand binding domain; Mammalian two hybrid; Nuclear receptors; Pioglitazone; PPAR; RXR; Salt bridge

Indexed keywords

PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; RECEPTOR SUBTYPE; RETINOID X RECEPTOR;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIMERIZATION; DNA BINDING; GENE MUTATION; LIGAND BINDING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RECEPTOR BINDING; WILD TYPE;

ANIMALS; BINDING SITES; CERCOPITHECUS AETHIOPS; COMPUTER SIMULATION; COS CELLS; DIMERIZATION; MICE; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NIH 3T3 CELLS; PPAR GAMMA; PROTEIN BINDING; PROTEIN CONFORMATION; RETINOID X RECEPTOR ALPHA; SALTS; STRUCTURE-ACTIVITY RELATIONSHIP;

MAMMALIA;

EID: 34249732441     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.05.051     Document Type: Article

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