1DFN

CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION

1DFN の概要

• エントリーDOI: 10.2210/pdb1dfn/pdb
• 分子名称: DEFENSIN HNP-3 (2 entities in total)
• 機能のキーワード: defensin
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P59665
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 6992.24

構造登録者

Hill, C.P.,Yee, J.,Selsted, M.E.,Eisenberg, D. (登録日: 1991-01-18, 公開日: 1992-07-15, 最終更新日: 2024-10-23)

主引用文献

Hill, C.P.,Yee, J.,Selsted, M.E.,Eisenberg, D.
Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization.
Science, 251:1481-1485, 1991

PubMed Abstract: Defensins (molecular weight 3500 to 4000) act in the mammalian immune response by permeabilizing the plasma membranes of a broad spectrum of target organisms, including bacteria, fungi, and enveloped viruses. The high-resolution crystal structure of defensin HNP-3 (1.9 angstrom resolution, R factor 0.19) reveals a dimeric beta sheet that has an architecture very different from other lytic peptides. The dimeric assembly suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.

PubMed: 2006422

実験手法

X-RAY DIFFRACTION (1.9 Å)