1ZA3

The crystal structure of the YSd1 Fab bound to DR5

1ZA3 の概要

• エントリーDOI: 10.2210/pdb1za3/pdb
• 関連するPDBエントリー: 1d0g
• 分子名称: Fab-YSd1 light chain, Fab-YSd1 heavy chain, Tumor necrosis factor receptor superfamily member 10B (3 entities in total)
• 機能のキーワード: phage display, protein engineering, combinatorial mutagenesis, antibody library, death receptor-5, immune system-signaling protein complex, immune system/signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: O14763
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 126742.72

構造登録者

Fellouse, F.A.,Li, B.,Compaan, D.M.,Peden, A.A.,Hymowitz, S.G.,Sidhu, S.S. (登録日: 2005-04-05, 公開日: 2005-06-14, 最終更新日: 2024-11-06)

主引用文献

Fellouse, F.A.,Li, B.,Compaan, D.M.,Peden, A.A.,Hymowitz, S.G.,Sidhu, S.S.
Molecular recognition by a binary code.
J.Mol.Biol., 348:1153-1162, 2005

PubMed Abstract: Functional antibodies were obtained from a library of antigen-binding sites generated by a binary code restricted to tyrosine and serine. An antibody raised against human vascular endothelial growth factor recognized the antigen with high affinity (K(D)=60 nM) and high specificity in cell-based assays. The crystal structure of another antigen binding fragment in complex with its antigen (human death receptor DR5) revealed the structural basis for this minimalist mode of molecular recognition. Natural antigen-binding sites are enriched for tyrosine and serine, and we show that these amino acid residues are intrinsically well suited for molecular recognition. Furthermore, these results demonstrate that molecular recognition can evolve from even the simplest chemical diversity.

PubMed: 15854651
DOI: 10.1016/j.jmb.2005.03.041

実験手法

X-RAY DIFFRACTION (3.35 Å)