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

doi:10.1016/0014-5793(95)00792-8

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^*

^*此作品的通信作者

研究成果: 雜誌貢獻 › 期刊論文 › 同行評審

46 引文斯高帕斯（Scopus）

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.

原文	英語
頁（從 - 到）	46-52
頁數	7
期刊	FEBS Letters
卷	370
發行號	1-2
DOIs	https://doi.org/10.1016/0014-5793(95)00792-8
出版狀態	已發佈 - 1995 8月 14
對外發佈	是

ASJC Scopus subject areas

生物物理學
結構生物學
生物化學
分子生物學
遺傳學
細胞生物學

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10.1016/0014-5793(95)00792-8

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

abstract = "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.",

keywords = "Antibacterial peptide, Endotoxin, Lipid A, NMR",

author = "Chinpan Chen and Roland Brock and Frederick Luh and Chou, {Ping Jung} and Larrick, {James W.} and Huang, {Rong Fong} and Huang, {Tai huang}",

note = "Funding Information: Acknowledgments. This work is supported by a grant from the National Science Council of the Republic of China (N SC83-0203-B001-102). We thank Mr. Jen-Ning Yang for performing CD spectral calibration.",

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doi = "10.1016/0014-5793(95)00792-8",

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AU - Chen, Chinpan

AU - Brock, Roland

AU - Luh, Frederick

AU - Chou, Ping Jung

AU - Larrick, James W.

AU - Huang, Rong Fong

AU - Huang, Tai huang

N1 - Funding Information: Acknowledgments. This work is supported by a grant from the National Science Council of the Republic of China (N SC83-0203-B001-102). We thank Mr. Jen-Ning Yang for performing CD spectral calibration.

PY - 1995/8/14

Y1 - 1995/8/14

N2 - 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.

AB - 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.

KW - Antibacterial peptide

KW - Endotoxin

KW - Lipid A

KW - NMR

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

摘要

ASJC Scopus subject areas

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