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. 1995 Aug 14;370(1-2):46-52.
doi: 10.1016/0014-5793(95)00792-8.

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

C Chen  1 , R Brock, F Luh, P J Chou, J W Larrick, R F Huang, T H Huang
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Free article

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

C Chen et al. FEBS Lett. .
Free article

Abstract

We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18(106-137), a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18(106-137) may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18(106-137) 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 CAP18(106-137) 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.

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