Structures of Xenopus embryonic epidermal lectin reveal a conserved mechanism of microbial glycan recognition

Journal of Biological Chemistry

Volumn 291, Issue 11, 2016, Pages 5596-5610

  Wangkanont, Kittikhun ^a   Wesener, Darryl A ^a   Vidani, Jack A ^a   Kiessling, Laura L ^a   Forest, Katrina T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIGEN-ANTIBODY REACTIONS; BACTERIA; BINDING ENERGY; BINDING SITES; BINS; COVALENT BONDS; IMMUNE SYSTEM; LIGANDS; MICROORGANISMS; OLIGOMERS; POLYSACCHARIDES;

CARBOHYDRATE-RECOGNITION DOMAINS; DOMAIN ARCHITECTURES; ENVIRONMENTAL WATER; INTERMOLECULAR DISULFIDE BOND; LIGAND BINDING MODE; LIGAND SPECIFICITY; QUATERNARY STRUCTURE; STREPTOCOCCUS PNEUMONIAE;

PROTEINS;

ALKENE DERIVATIVE; CALCIUM ION; CARBOHYDRATE; EMBRYONIC EPIDERMAL LECTIN; GLYCAN; GLYCEROPHOSPHATE; INTELECTIN 1; LECTIN; UNCLASSIFIED DRUG; VICINAL DIOL; BACTERIAL POLYSACCHARIDE; CYTOKINE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; ITLN1 PROTEIN, HUMAN; POLYSACCHARIDE; XEEL PROTEIN, XENOPUS;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; CELL AGGLUTINATION; COMPLEX FORMATION; CONTROLLED STUDY; DISULFIDE BOND; EMBRYO; INNATE IMMUNITY; LIGAND BINDING; MOLECULAR RECOGNITION; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; STREPTOCOCCUS PNEUMONIAE; XENOPUS LAEVIS; ANIMAL; CHEMISTRY; CYTOLOGY; HUMAN; METABOLISM; MICROBIOLOGY; MOLECULAR GENETICS; MOLECULAR MODEL; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; CYTOKINES; GPI-LINKED PROTEINS; HUMANS; LECTINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYSACCHARIDES; POLYSACCHARIDES, BACTERIAL; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STREPTOCOCCUS PNEUMONIAE; XENOPUS LAEVIS;

EID: 84958266691     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.709212     Document Type: Article

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