- Protein Classification
- Protein Links
| 1lfc » Lactoferricin B, peptide 36-60 | |
|---|---|
| Hydrophobic Thickness or Depth | 4.6 ± 0.5 Å |
| Tilt Angle | 90 ± 6° |
| ΔGtransfer | -5.3 kcal/mol |
| Links to 1lfc | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | out |
| Resolution | NMR |
| Other PDB entries representing this structure | none |
| Number of subunits | 1 |
| Experimental Verification for 1lfc » Lactoferricin B, peptide 36-60 |
|---|
| The calculated orientation is in agreement with fluorescence of two Trp residues (Schibli et al. 2002, Nguyen et al. 2005). |
| 3 references |
|---|
| Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., Vogel H.J. 1998. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 37:4288-4298(1998). PubMed |
| Nguyen, L.T., Schibli, D.J., and Vogel, H.J. 2005. Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin. J. Pept. Sci. 11:379-389. PubMed |
| Schibli DJ, Epand RF, Vogel HJ, Epand RM. 2002. Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions. Biochem Cell Biol. 80: 667-677. PubMed |
| Comments on 1lfc » Lactoferricin B, peptide 36-60 |
|---|
| This is structure in water. This is an antimicrobial peptide released by pepsin cleavage of lactoferrin, an 80 kDa iron-binding glycoprotein with many immunologically important functions. The NMR structure of LfcinB reveals a somewhat distorted antiparallel beta-sheet. This contrasts with the X-ray structure of bovine lactoferrin, in which residues 1-13 (of LfcinB) form an alpha-helix (Hwang et al. 1998). Human lactoferricin (1z6v, 1z6w) also forms an alpha-helix. A six-residue segment of bovine lactoferricin was studied in SDS micelles (1y58, 1y5c). |
