The 1.5 Å crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding

Journal of Biological Chemistry

Volumn 285, Issue 52, 2010, Pages 40762-40770

  Park, HaJeung ^a   Boyington, Jeffrey C ^a,b  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

^b NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCTS; BINDING PROPERTIES; EXTRACELLULAR DOMAINS; GEL SHIFT ASSAYS; HUMAN RECEPTORS; HYDROPHOBIC INTERACTIONS; HYDROPHOBIC PATCH; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; MULTIPLE LIGANDS; NEGATIVE CHARGE; NEURODEGENERATIVE DISORDERS; PATTERN RECOGNITION RECEPTORS; SIGNALING EVENTS; STRUCTURAL FEATURE; UNIQUE FEATURES;

BINDING ENERGY; HYDROPHOBICITY; LIGANDS; PATTERN RECOGNITION; PROTEINS;

CRYSTAL STRUCTURE;

ADVANCED GLYCATION END PRODUCT; ADVANCED GLYCATION END PRODUCT RECEPTOR; CALCIUM ION; DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; PROTEIN S100B;

ARTICLE; CRYSTAL STRUCTURE; HUMAN; HYDROPHOBICITY; LIGAND BINDING; PLASMID; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN PURIFICATION; SIGNAL TRANSDUCTION;

ANTIGENS, NEOPLASM; CRYSTALLOGRAPHY, X-RAY; DNA; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LIGANDS; MITOGEN-ACTIVATED PROTEIN KINASES; NERVE GROWTH FACTORS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RNA, DOUBLE-STRANDED; S100 PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 78650341420     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.169276     Document Type: Article

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