Structure, function, and membrane integration of defensins.
Defensins comprise a structural class of small cationic peptides that exert broad-spectrum antimicrobial activities through membrane permeabilization. Their predominantly beta-sheet structure, stabilized by three disulfide bonds, distinguishes them from other antimicrobial peptides which typically form amphiphilic helices. Defensins bind to membranes electrostatically and subsequently form apparently multimeric pores. Recent structural and biophysical studies are beginning to provide insights into the process of permeabilization.
Department of Physiology and Biophysics, University of California, Irvine 92717-4560, USA.
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White
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Wimley
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Selsted
D000595:Amino Acid Sequence; D000818:Animals; D001770:Blood Bactericidal Activity; D001798:Blood Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism; D023082:Defensins; D006801:Humans; D016982:Micrococcus luteus; D008969:Molecular Sequence Data; D013329:Structure-Activity Relationship
D001798:Blood Proteins; D023082:Defensins