1xv7: Difference between revisions

Revision as of 14:42, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xv7.png

Template:STRUCTURE 1xv7

Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micellesSolution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles

Template:ABSTRACT PUBMED 15687491

About this StructureAbout this Structure

Full experimental information is available from OCA.

ReferenceReference

Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide., Japelj B, Pristovsek P, Majerle A, Jerala R, J Biol Chem. 2005 Apr 29;280(17):16955-61. Epub 2005 Feb 1. PMID:15687491

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-'''Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles'''
+===Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles===
-==Overview==
+<!--
-Treatment of Gram-negative bacterial infections with antimicrobial agents can cause release of the endotoxin lipopolysaccharide (LPS), the potent initiator of sepsis, which is the major cause of mortality in intensive care units worldwide. Structural information on peptides bound to LPS can lead to the development of more effective endotoxin neutralizers. Short linear antimicrobial and endotoxin-neutralizing peptide LF11, based on the human lactoferrin, binds to LPS, inducing a peptide fold with a "T-shaped" arrangement of a hydrophobic core and two clusters of basic residues that match the distance between the two phosphate groups of LPS. Side chain arrangement of LF11 bound to LPS extends the previously proposed LPS binding pattern, emphasizing the importance of both electrostatic and hydrophobic interactions in a defined geometric arrangement. In anionic micelles, the LF11 forms amphipathic conformation with a smaller hydrophobic core than in LPS, whereas in zwitterionic micelles, the structure is even less defined. Protection of tryptophan fluorescence quenching in the order SDS&gt;LPS&gt;DPC and hydrogen exchange protection indicates the decreasing extent of insertion of the N terminus and potential role of peptide plasticity in differentiation between bacterial and eukaryotic membranes.
+The line below this paragraph, {{ABSTRACT_PUBMED_15687491}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15687491 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15687491}}
 ==About this Structure==
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV7 OCA].
+Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV7 OCA].
 ==Reference==
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 [[Category: Hydrophobic core]]
 [[Category: Loop]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:32:56 2008''
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