Functional determinants of human enteric α-defensin HD5: Crucial role for hydrophobicity at dimer interface

Journal of Biological Chemistry

Volumn 287, Issue 26, 2012, Pages 21615-21627

  Rajabi, Mohsen ^a   Ericksen, Bryan ^a   Wu, Xueji ^a   De Leeuw, Erik ^a   Zhao, Le ^a   Pazgier, Marzena ^a   Lu, Wuyuan ^a  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE-SCANNING MUTAGENESIS; AMINOBUTYRIC ACIDS; ANTI-BACTERIAL ACTIVITY; AROMATIC SUBSTITUTIONS; BACTERICIDAL ACTIVITY; CATIONIC PEPTIDES; COLONY COUNTS; DEFENSINS; DIMER INTERFACE; HIGHER ORDER; HUMAN NEUTROPHIL; HYDROPHOBIC CONTACT; HYDROPHOBIC RESIDUES; LETHAL FACTOR; N-METHYLATION; NORLEUCINE; PROTEIN TOXINS; S. AUREUS; STAPHYLOCOCCUS AUREUS; WILD TYPES;

ALKYLATION; AMINO ACIDS; BACTERIA; BACTERICIDES; DIMERIZATION; DIMERS; ENZYME ACTIVITY; ENZYME INHIBITION; ESCHERICHIA COLI; PEPTIDES;

HYDROPHOBICITY;

4 AMINOBUTYRIC ACID; ALANINE; ALPHA DEFENSIN; ANTHRAX LETHAL FACTOR; ANTHRAX TOXIN; DIMER; GLUTAMIC ACID; LEUCINE; MONOMER; NORLEUCINE; PEPTIDE; PROTEIN HD5; PROTEIN HNP1; TRYPTOPHAN; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL BINDING; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME INHIBITION; ENZYME KINETICS; ESCHERICHIA COLI; HYDROPHOBICITY; METHYLATION; MUTAGENESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN METHYLATION; STAPHYLOCOCCUS AUREUS; SURFACE PLASMON RESONANCE; X RAY CRYSTALLOGRAPHY;

ALANINE; ALPHA-DEFENSINS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INHIBITORY CONCENTRATION 50; KINETICS; LEUCINE; MOLECULAR CONFORMATION; MUTAGENESIS; MUTATION; PEPTIDES; PROTEIN CONFORMATION; STAPHYLOCOCCUS AUREUS; SURFACE PLASMON RESONANCE;

EID: 84862679509     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.367995     Document Type: Article

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