Bead-linked proteoliposomes: A reconstitution method for NMR analyses of membrane protein-ligand interactions

Mariko Yokogawa, Koh Takeuchi, Ichio Shimada

研究成果: Article査読

23 被引用数 (Scopus)

抄録

Structural information about the interactions between membrane proteins and their ligands provides insights into the membrane protein functions. A variety of surfactants have been used for structural analyses of membrane proteins, and in some cases, they yielded successful results. However, the use of surfactants frequently increases the conformational instability of membrane proteins and distorts their normal function. Here, we propose a new strategy of membrane protein reconstitution into lipid bilayers on affinity beads, which maintains the native conformation and function of the protein for NMR studies. The reconstituted membrane proteins are suitable for NMR analyses of interactions, by using the transferred cross-saturation method. The strategy was successfully applied to the interaction between a potassium ion channel, KcsA, and a pore-blocker, agitoxin2 (AgTx2). This strategy would be useful for analyzing the interactions between various membrane proteins and their ligands.

本文言語English
ページ(範囲)12021-12027
ページ数7
ジャーナルJournal of the American Chemical Society
127
34
DOI
出版ステータスPublished - 2005 8月 31
外部発表はい

ASJC Scopus subject areas

  • 触媒
  • 化学 (全般)
  • 生化学
  • コロイド化学および表面化学

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