1EWS

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE RABBIT KIDNEY DEFENSIN, RK-1

1EWS の概要

• エントリーDOI: 10.2210/pdb1ews/pdb
• 分子名称: RK-1 DEFENSIN (1 entity in total)
• 機能のキーワード: alpha defensin, triple-stranded beta-sheet, antimicrobial protein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3712.39

構造登録者

McManus, A.M.,Dawson, N.F.,Wade, J.D.,Craik, D.J. (登録日: 2000-04-26, 公開日: 2001-05-02, 最終更新日: 2022-02-16)

主引用文献

McManus, A.M.,Dawson, N.F.,Wade, J.D.,Carrington, L.E.,Winzor, D.J.,Craik, D.J.
Three-dimensional structure of RK-1: a novel alpha-defensin peptide.
Biochemistry, 39:15757-15764, 2000

PubMed Abstract: NMR spectroscopy and simulated annealing calculations have been used to determine the three-dimensional structure of RK-1, an antimicrobial peptide from rabbit kidney recently discovered from homology screening based on the distinctive physicochemical properties of the corticostatins/defensins. RK-1 consists of 32 residues, including six cysteines arranged into three disulfide bonds. It exhibits antimicrobial activity against Escherichia coli and activates Ca(2+) channels in vitro. Through its physicochemical similarity, identical cysteine spacing, and linkage to the corticostatins/defensins, it was presumed to be a member of this family. However, RK-1 lacks both a large number of arginines in the primary sequence and a high overall positive charge, which are characteristic of this family of peptides. The three-dimensional solution structure, determined by NMR, consists of a triple-stranded antiparallel beta-sheet and a series of turns and is similar to the known structures of other alpha-defensins. This has enabled the definitive classification of RK-1 as a member of this family of antimicrobial peptides. Ultracentrifuge measurements confirmed that like rabbit neutrophil defensins, RK-1 is monomeric in solution, in contrast to human neutrophil defensins, which are dimeric.

PubMed: 11123900
DOI: 10.1021/bi000457l

実験手法

SOLUTION NMR