1lfc
From Proteopedia
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BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES
Overview
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.
About this Structure
1LFC is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin., Hwang PM, Zhou N, Shan X, Arrowsmith CH, Vogel HJ, Biochemistry. 1998 Mar 24;37(12):4288-98. PMID:9521752
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