1LFC

BOVINE LACTOFERRICIN (LFCINB), NMR, 20 STRUCTURES

1LFC の概要

• エントリーDOI: 10.2210/pdb1lfc/pdb
• NMR情報: BMRB: 4157
• 分子名称: LACTOFERRICIN (1 entity in total)
• 機能のキーワード: antimicrobial peptide, proteolytic fragment, iron transport
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P24627
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3133.85

構造登録者

Hwang, P.M.,Zhou, N.,Shan, X.,Arrowsmith, C.H.,Vogel, H.J. (登録日: 1998-06-24, 公開日: 1998-11-04, 最終更新日: 2024-10-23)

主引用文献

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

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: 9521752
DOI: 10.1021/bi972323m

実験手法

SOLUTION NMR