1SVX

Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein

1SVX の概要

• エントリーDOI: 10.2210/pdb1svx/pdb
• 関連するPDBエントリー: 1MJ0
• 分子名称: Ankyrin Repeat Protein off7, Maltose-binding periplasmic protein (3 entities in total)
• 機能のキーワード: ankyrin repeat protein, selected binder, protein design, artificial complex, de novo protein-sugar binding protein complex, de novo protein/sugar binding protein
• 細胞内の位置: Periplasm: P02928
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61496.18

構造登録者

Binz, H.K.,Amstutz, P.,Kohl, A.,Stumpp, M.T.,Briand, C.,Forrer, P.,Gruetter, M.G.,Plueckthun, A. (登録日: 2004-03-30, 公開日: 2004-05-25, 最終更新日: 2024-02-14)

主引用文献

Binz, H.K.,Amstutz, P.,Kohl, A.,Stumpp, M.T.,Briand, C.,Forrer, P.,Gruetter, M.G.,Plueckthun, A.
High-affinity binders selected from designed ankyrin repeat protein libraries
NAT.BIOTECHNOL., 22:575-582, 2004

PubMed Abstract: We report here the evolution of ankyrin repeat (AR) proteins in vitro for specific, high-affinity target binding. Using a consensus design strategy, we generated combinatorial libraries of AR proteins of varying repeat numbers with diversified binding surfaces. Libraries of two and three repeats, flanked by 'capping repeats,' were used in ribosome-display selections against maltose binding protein (MBP) and two eukaryotic kinases. We rapidly enriched target-specific binders with affinities in the low nanomolar range and determined the crystal structure of one of the selected AR proteins in complex with MBP at 2.3 A resolution. The interaction relies on the randomized positions of the designed AR protein and is comparable to natural, heterodimeric protein-protein interactions. Thus, our AR protein libraries are valuable sources for binding molecules and, because of the very favorable biophysical properties of the designed AR proteins, an attractive alternative to antibody libraries.

PubMed: 15097997
DOI: 10.1038/nbt962

実験手法

X-RAY DIFFRACTION (2.24 Å)