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

FEBS Letters

Chou, Ping-Jung¹  Huang, Tai-huang¹  Brock, Roland¹  Luh, Frederick¹  Larrick, James W.²  Huang, Rong-Fong¹  Chen, Chinpan¹ 

[1] Division of Structural Biology, Institute of Biomedical Sciences, Academia Sinica, Nankang, Taipei 11529, Taiwan, ROC;Palo Alto Institute of Molecular Medicine, Mountain View, CA 94043, USA

关键词: Lipid A;    Antibacterial peptide;    Endotoxin;    NMR;   

DOI  :  10.1016/0014-5793(95)00792-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown