A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins.
A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins.
复制标题
原核和真核蛋白质识别脂多糖的保守结构基序。
DOI：
10.1016/s0969-2126(00)00143-x
复制
发表时间：
2000
期刊：
影响因子：
5.7
通讯作者：
K. Diederichs
中科院分区：
文献类型：
--
作者：
A. Ferguson;W. Welte;E. Hofmann;B. Lindner;O. Holst;J. Coulton;K. Diederichs
Background:Lipopolysaccharide (LPS), a lipoglycan from the outer membrane of Gram-negative bacteria, is an immunomodulatory molecule that stimulates the innate immune response. High levels of LPS cause excessive release of inflammatory mediators and are responsible for the septic shock syndrome. The interaction of LPS with its cognate binding proteins has not, as yet, been structurally elucidated.Results:The X-ray crystallographic structure of LPS in complex with the integral outer membrane protein FhuA fromEscherichia coliK-12 is reported. It is in accord with data obtained using mass spectroscopy and nuclear magnetic resonance. Most of the important hydrogen-bonding or electrostatic interactions with LPS are provided by eight positively charged residues of FhuA. Residues in a similar three-dimensional arrangement were searched for in all structurally known proteins using a fast template-matching algorithm, and a subset of four residues was identified that is common to known LPS-binding proteins.Conclusions:These four residues, three of which form specific interactions with lipid A, appear to provide the structural basis of pattern recognition in the innate immune response. Their arrangement can serve to identify LPS-binding sites on proteins known to interact with LPS, and could serve as a template for molecular modeling of a LPS scavenger designed to reduce the septic shock syndrome.
影响因子：
5.6
作者：
ANDERSON, BF;BAKER, HM;BAKER, EN
通讯作者：
BAKER, EN
影响因子：
64.8
作者：
GRUTTER, MG;WEAVER, LH;MATTHEWS, BW
通讯作者：
MATTHEWS, BW