Structure of protein having inhibitory disintegrin and leukotriene scavenging functions contained in single domain

Journal of Biological Chemistry

Volumn 287, Issue 14, 2012, Pages 10967-10976

  Xu, Eqing ^a   Francischetti, Ivo M B ^a   Lai, Ren ^b   Ribeiro, José M C ^a   Andersen, John F ^a  

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

^b KUNMING INSTITUTE OF ZOOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-INFLAMMATORIES; ARG GLY ASPS; CHANNEL ENTRANCES; DELIPIDATION; EICOSANOIDS; FATTY ACID CHAINS; FATTY-ACID MOLECULES; HYDROPHOBIC POCKETS; INTEGRINS; POLAR SIDE CHAINS; PROINFLAMMATORY; RGD MOTIF; RGD SEQUENCES; SINGLE DOMAINS; SUB-MICROMOLAR AFFINITY; TRIPEPTIDE; TURN STRUCTURE; TYPE II; X RAY CRYSTAL STRUCTURES;

AMINO ACIDS; CARBOXYLATION; ESCHERICHIA COLI; HYDROGEN; HYDROPHOBICITY; LIGANDS; SCAVENGING;

PROTEINS;

CILENGITIDE; DISINTEGRIN; FATTY ACID; LEUKOTRIENE C4; LEUKOTRIENE D4; LEUKOTRIENE E4; PEPTIDOLEUKOTRIENE; SCAVENGER; SECRETORY PROTEIN; TABLYSIN 15; UNCLASSIFIED DRUG; VITRONECTIN RECEPTOR;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BETA SHEET; BETA TURN; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL ACTIVATION; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; ENDOTHELIUM CELL; GUINEA PIG; HUMAN; HYDROGEN BOND; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN MOTIF; PROTEIN PURIFICATION; RECEPTOR BINDING; RGD MOTIF; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; THROMBOCYTE AGGREGATION INHIBITION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; DISINTEGRINS; FATTY ACIDS; HUMANS; INSECT PROTEINS; INTEGRINS; LEUKOTRIENES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PLATELET AGGREGATION; PROTEIN STRUCTURE, TERTIARY; SALIVARY PROTEINS AND PEPTIDES;

ESCHERICHIA COLI;

EID: 84859499792     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.340471     Document Type: Article

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