1Z6V

Human lactoferricin

1Z6V の概要

• エントリーDOI: 10.2210/pdb1z6v/pdb
• 関連するPDBエントリー: 1LFC
• 分子名称: Lactotransferrin (1 entity in total)
• 機能のキーワード: helical, antimicrobial peptide, membrane mimetic solvent, antimicrobial protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P02788
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5754.75

構造登録者

Hunter, H.N.,Demcoe, A.R.,Jenssen, H.,Gutteberg, T.J.,Vogel, H.J. (登録日: 2005-03-23, 公開日: 2005-08-16, 最終更新日: 2022-03-02)

主引用文献

Hunter, H.N.,Demcoe, A.R.,Jenssen, H.,Gutteberg, T.J.,Vogel, H.J.
Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent
ANTIMICROB.AGENTS CHEMOTHER., 49:3387-3395, 2005

PubMed Abstract: Lactoferricins are highly basic bioactive peptides that are released in the stomach through proteolytic cleavage of various lactoferrin proteins. Here we have determined the solution structure of human lactoferricin (LfcinH) by conventional two-dimensional nuclear magnetic resonance methods in both aqueous solution and a membrane mimetic solvent. Unlike the 25-residue bovine lactoferricin (LfcinB), which adopts a somewhat distorted antiparallel beta sheet, the longer LfcinH peptide shows a helical content from Gln14 to Lys29 in the membrane mimetic solvent but a nonexistent beta-sheet character in either the N- or C-terminal regions of the peptide. The helical characteristic of the LfcinH peptide resembles the conformation that this region adopts in the crystal structure of the intact protein. The LfcinH structure determined in aqueous solution displays a nascent helix in the form of a coiled conformation in the region from Gln14 to Lys29. Numerous hydrophobic interactions create the basis for the better-defined overall structure observed in the membrane mimetic solvent. The 49-residue LfcinH peptide isolated for these studies was found to be slightly longer than previously reported peptide preparations and was found to have an intact peptide bond between residues Ala11 and Val12. The distinct solution structures of LfcinH and LfcinB represent a novel difference in the physical properties of these two peptides, which contributes to their unique physiological activities.

PubMed: 16048952
DOI: 10.1128/AAC.49.8.3387-3395.2005

実験手法

SOLUTION NMR