1u62
From Proteopedia
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- | [[Image:1u62.gif|left|200px]] | + | [[Image:1u62.gif|left|200px]] |
- | + | ||
- | '''NMR structure analysis of the lactoferrin-based peptide FQWQRNIRKVR in complex with lipopolysaccharide''' | + | {{Structure |
+ | |PDB= 1u62 |SIZE=350|CAPTION= <scene name='initialview01'>1u62</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''NMR structure analysis of the lactoferrin-based peptide FQWQRNIRKVR in complex with lipopolysaccharide''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1U62 is a [ | + | 1U62 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U62 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:// | + | 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: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Japelj, B.]] | [[Category: Japelj, B.]] | ||
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[[Category: tranferred noe]] | [[Category: tranferred noe]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:27:45 2008'' |
Revision as of 12:27, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
NMR structure analysis of the lactoferrin-based peptide FQWQRNIRKVR in complex with lipopolysaccharide
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>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 Structure
1U62 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
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:15687491
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