1LFC
BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES
Summary for 1LFC
| Entry DOI | 10.2210/pdb1lfc/pdb |
| NMR Information | BMRB: 4157 |
| Descriptor | LACTOFERRICIN (1 entity in total) |
| Functional Keywords | antimicrobial peptide, proteolytic fragment, iron transport |
| Biological source | Bos taurus (cattle) |
| Cellular location | Secreted: P24627 |
| Total number of polymer chains | 1 |
| Total formula weight | 3133.85 |
| Authors | Hwang, P.M.,Zhou, N.,Shan, X.,Arrowsmith, C.H.,Vogel, H.J. (deposition date: 1998-06-24, release date: 1998-11-04, Last modification date: 2024-10-23) |
| Primary citation | Hwang, P.M.,Zhou, N.,Shan, X.,Arrowsmith, C.H.,Vogel, H.J. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry, 37:4288-4298, 1998 Cited by PubMed Abstract: The solution structure of bovine lactoferricin (LfcinB) has been determined using 2D 1H NMR spectroscopy. LfcinB is a 25-residue 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. Hence, this region of lactoferricin B appears able to adopt a helical or sheetlike conformation, similar to what has been proposed for the amyloidogenic prion proteins and Alzheimer's beta-peptides. LfcinB has an extended hydrophobic surface comprised of residues Phe1, Cys3, Trp6, Trp8, Pro16, Ile18, and Cys20. The side chains of these residues are well-defined in the NMR structure. Many hydrophilic and positively charged residues surround the hydrophobic surface, giving LfcinB an amphipathic character. LfcinB bears numerous similarities to a vast number of cationic peptides which exert their antimicrobial activities through membrane disruption. The structures of many of these peptides have been well characterized, and models of their membrane-permeabilizing mechanisms have been proposed. The NMR solution structure of LfcinB may be more relevant to membrane interaction than that suggested by the X-ray structure of intact lactoferrin. Based on the solution structure, it is now possible to propose potential mechanisms for the antimicrobial action of LfcinB. PubMed: 9521752DOI: 10.1021/bi972323m PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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