The solution structure of the active domain of CAP18 - a lipopolysaccharide binding protein from rabbit leukocytes

Chinpan Chen, Roland Brock, Frederick Luh, Ping Jung Chou, James W. Larrick, Rong Fong Huang, Tai huang Huang

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We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18106-137, a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18106-137 may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18106-137 in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18106-137 are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains.

Original languageEnglish
Pages (from-to)46-52
Number of pages7
JournalFEBS Letters
Issue number1-2
Publication statusPublished - 1995 Aug 14



  • Antibacterial peptide
  • Endotoxin
  • Lipid A
  • NMR

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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