Specific ligand binding domain residues confer low dioxin responsiveness to AHR1β of xenopus laevis

Biochemistry

Volumn 52, Issue 10, 2013, Pages 1746-1754

  Odio, Camila ^a,e   Holzman, Sarah A ^a,f   Denison, Michael S ^b   Fraccalvieri, Domenico ^c   Bonati, Laura ^c   Franks, Diana G ^d   Hahn, Mark E ^d   Powell, Wade H ^a  

^a KENYON COLLEGE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF MILANO BICOCCA   (Italy)

^d WOODS HOLE OCEANOGRAPHIC INSTITUTION   (United States)

^e CLEVELAND CLINIC LERNER COLLEGE OF MEDICINE   (United States)

^f EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 ,3 ,7 ,8 TETRACHLORODIBENZO P DIOXINS; AMINO ACID RESIDUES; ARYL HYDROCARBON RECEPTOR; COMPARATIVE STUDIES; LIGAND BINDING DOMAIN; SEDIMENTATION ANALYSIS; SIDE-CHAIN INTERACTIONS; STRUCTURAL FEATURE;

AMINO ACIDS; LIGANDS; PROTEINS;

MAMMALS;

2,3,7,8 TETRACHLORODIBENZO PARA DIOXIN; 6 FORMYLINDOLO[3,2 B]CARBAZOLE; AMINO ACID; AROMATIC HYDROCARBON RECEPTOR; ARYL HYDROCARBON RECEPTOR 1BETA; CARBAZOLE DERIVATIVE; HYPOXIA INDUCIBLE FACTOR 1BETA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; LIGAND; SERINE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; LIGAND BINDING; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE; SEDIMENTATION RATE; SENSITIVITY ANALYSIS; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTORS; BINDING SITES; CARBAZOLES; LIGANDS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ARYL HYDROCARBON; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; TETRACHLORODIBENZODIOXIN; TRANSCRIPTIONAL ACTIVATION; XENOPUS LAEVIS; XENOPUS PROTEINS;

EID: 84875003032     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301722k     Document Type: Article

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