Display Settings:

Format

Send to:

Choose Destination
    Curr Opin Struct Biol. 1995 Aug;5(4):521-7.

    Structure, function, and membrane integration of defensins.

    Source

    Department of Physiology and Biophysics, University of California, Irvine 92717-4560, USA.

    Abstract

    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.

    PMID:
    8528769
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Icon for Elsevier Science

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk