1LP1

Protein Z in complex with an in vitro selected affibody

1LP1 の概要

• エントリーDOI: 10.2210/pdb1lp1/pdb
• 関連するPDBエントリー: 2spz
• 分子名称: Affibody binding protein Z, Immunoglobulin G binding protein A, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: in vitro evolved, protein-protein complex, three-helix bundle, affibody, immune system
• 由来する生物種: Staphylococcus aureus; 詳細
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : P38507
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13504.14

構造登録者

Hogbom, M.,Eklund, M.,Nygren, P.A.,Nordlund, P. (登録日: 2002-05-07, 公開日: 2003-03-18, 最終更新日: 2023-10-25)

主引用文献

Hogbom, M.,Eklund, M.,Nygren, P.A.,Nordlund, P.
Structural basis for recognition by an in vitro evolved affibody.
Proc.Natl.Acad.Sci.USA, 100:3191-3196, 2003

PubMed Abstract: The broad binding repertoire of antibodies has permitted their use in a wide range of applications. However, some uses of antibodies are precluded due to limitations in the efficiency of antibody generation. In vitro evolved binding proteins, selected from combinatorial libraries generated around various alternative structural scaffolds, are promising alternatives to antibodies. We have solved the crystal structure of a complex of an all alpha-helical in vitro selected binding protein (affibody) bound to protein Z, an IgG Fc-binding domain derived from staphylococcal protein A. The structure of the complex reveals an extended and complementary binding surface with similar properties to protein-antibody interactions. The surface region of protein Z recognized by the affibody is strikingly similar to the one used for IgG(1) Fc binding, suggesting that this surface contains potential hot-spots for binding. The implications of the selected affibody binding-mode for its application as a universal binding protein are discussed.

PubMed: 12604795
DOI: 10.1073/pnas.0436100100

実験手法

X-RAY DIFFRACTION (2.3 Å)