1xv7: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1xv7.gif|left|200px]] | [[Image:1xv7.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1xv7", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1xv7| PDB=1xv7 | SCENE= }} | |||
}} | |||
'''Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles''' | '''Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV7 OCA]. | |||
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/15687491 15687491] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15687491 15687491] | ||
[[Category: Japelj, B.]] | [[Category: Japelj, B.]] | ||
[[Category: Jerala, R.]] | [[Category: Jerala, R.]] | ||
[[Category: Majerle, A.]] | [[Category: Majerle, A.]] | ||
[[Category: Pristovsek, P.]] | [[Category: Pristovsek, P.]] | ||
[[Category: | [[Category: Hydrophobic core]] | ||
[[Category: | [[Category: Loop]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:32:56 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 15:32, 3 May 2008
Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles
OverviewOverview
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>LPS>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.
About this StructureAbout this Structure
Full crystallographic 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 Page seeded by OCA on Sat May 3 15:32:56 2008