Structure determination of human and murine β-defensins reveals structural conservation in the absence of significant sequence similarity

Protein Science

Volumn 10, Issue 12, 2001, Pages 2470-2479

  Bauer, Finn ^a   Schweimer, Kristian ^a,c   Klüver, Enno ^b   Conejo Garcia, Jose Ramon ^b   Forssmann, Wolf Georg ^b   Rösch, Paul ^a   Adermann, Knut ^b   Sticht, Heinrich ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b IPF PHARMACEUTICALS GMBH   (Germany)

^c Novaspin Biotech GmbH   (Germany)

Author keywords

defensin; Antimicrobial peptide; Chemokine receptor; Chemotaxis; NMR structure; Peptide fold

Indexed keywords

DEFENSIN;

AMINO ACID SEQUENCE; ANTIBACTERIAL ACTIVITY; ARTICLE; DISULFIDE BOND; HUMAN; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BETA-DEFENSINS; CHROMATOGRAPHY; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); MAMMALIA; MURINAE;

EID: 0035188391     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.24401     Document Type: Article

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