› 2k98

Solution NMR

Helical hairpin structure of potent antimicrobial peptide MSI-594 in the presence of Lipopolysaccharide micelle

Released:
DOI: 10.2210/pdb2k98/pdb
PDB entry 2k98 coloured by chain, ensemble of 20 models, front view.
PDB entry 2k98 coloured by chain, ensemble of 20 models, side view.
PDB entry 2k98 coloured by chain, ensemble of 20 models, top view.
Source organism: Synthetic construct
Primary publication:
Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy.
Bhunia A, Ramamoorthy A, Bhattacharjya S
Chemistry 15 2036-40 (2009)
PMID: 19180607

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162807 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MSI-594 Chain: A
Molecule details ›
Chain: A
Length: 24 amino acids
Theoretical weight: 2.45 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Not provided

Quick links

Citations

11 review citations

Cationic amphiphiles, a new generation of antimicrobials inspired by the natural antimicrobial peptide scaffold.
Findlay et al. (2010)
10 more

3 mentions without citation

Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control.
Datta et al. (2016)
2 more