MD-2 residues tyrosine 42, arginine 69, aspartic acid 122, and leucine 125 provide species specificity for lipid IVA

Journal of Biological Chemistry

Volumn 285, Issue 36, 2010, Pages 27935-27943

  Meng, Jianmin ^a   Drolet, Joshua R ^a   Monks, Brian G ^a   Golenbock, Douglas T ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHARGED PARTICLES; ENZYME ACTIVITY; IMMUNOLOGY; ORGANIC ACIDS; PHOSPHATASES; SURFACE CHARGE; VEHICULAR TUNNELS;

AGONIST ACTIVITY; ASPARTIC ACIDS; CELLULAR RESPONSE; CHARGE DIFFERENCE; HUMAN CELLS; HYDROPHOBIC POCKETS; INNATE IMMUNE RESPONSE; LIPOPOLYSACCHARIDES; SINGLE MUTATION; SITE DIRECTED MUTAGENESIS; SPECIFIC SURFACE; SYNTHETIC LIPID; TOLL-LIKE RECEPTOR 4;

DIMERIZATION;

ARGININE; ASPARTIC ACID; LEUCINE; LIPID; LIPOPOLYSACCHARIDE; PROTEIN MD 2; TOLL LIKE RECEPTOR 4; TYROSINE; GLYCOLIPID; LIPID A; LIPID A PRECURSORS, BACTERIAL; PROTEIN BINDING;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; GENE MUTATION; HUMAN; HUMAN CELL; HYDROGEN BOND; HYDROPHOBICITY; MOUSE; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; SPECIES DIFFERENCE; STATIC ELECTRICITY; SURFACE CHARGE; ANALOGS AND DERIVATIVES; ANIMAL; CELL LINE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE;

MURINAE; MUS;

ANIMALS; ARGININE; ASPARTIC ACID; CELL LINE; GLYCOLIPIDS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LEUCINE; LIPID A; LYMPHOCYTE ANTIGEN 96; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENOTYPE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; SPECIES SPECIFICITY; STATIC ELECTRICITY; TOLL-LIKE RECEPTOR 4; TYROSINE;

EID: 77956241008     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.134668     Document Type: Article

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