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A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins

A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins

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Prüfsumme: MD5:417e505e4e77778d97d2df20ce24ee15

FERGUSON, Andrew D., Wolfram WELTE, Eckhard HOFMANN, Buko LINDNER, Otto HOLST, James W. COULTON, Kay DIEDERICHS, 2000. A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. In: Structure. 8(6), pp. 585-592. ISSN 0969-2126. Available under: doi: 10.1016/S0969-2126(00)00143-X

@article{Ferguson2000conse-8098, title={A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins}, year={2000}, doi={10.1016/S0969-2126(00)00143-X}, number={6}, volume={8}, issn={0969-2126}, journal={Structure}, pages={585--592}, author={Ferguson, Andrew D. and Welte, Wolfram and Hofmann, Eckhard and Lindner, Buko and Holst, Otto and Coulton, James W. and Diederichs, Kay} }

A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins deposit-license 2011-03-24T17:39:55Z Lindner, Buko 2000 Coulton, James W. Ferguson, Andrew D. Diederichs, Kay Welte, Wolfram First publ. in: Structure 8 (2000), pp. 585-592 eng Hofmann, Eckhard Lindner, Buko Holst, Otto Ferguson, Andrew D. Holst, Otto Coulton, James W. Hofmann, Eckhard 2011-03-24T17:39:55Z 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.<br /><br />Results: The X-ray crystallographic structure of LPS in complex with the integralouter membrane protein FhuA from Escherichia coli K-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.<br /><br />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. Welte, Wolfram Diederichs, Kay application/pdf

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