6XR2

Computationally designed right-handed alpha/alpha homotrimeric toroid with 3 repeats per subunit

6XR2 の概要

• エントリーDOI: 10.2210/pdb6xr2/pdb
• 分子名称: dTor_3x57R (2 entities in total)
• 機能のキーワード: computationally designed, de novo, toroid, helix-turn-helix, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 113709.04

構造登録者

Hallinan, J.P.,Doyle, L.,Bradley, P.,Stoddard, B.L. (登録日: 2020-07-10, 公開日: 2021-07-14, 最終更新日: 2024-05-22)

主引用文献

Hallinan, J.P.,Doyle, L.A.,Shen, B.W.,Gewe, M.M.,Takushi, B.,Kennedy, M.A.,Friend, D.,Roberts, J.M.,Bradley, P.,Stoddard, B.L.
Design of functionalised circular tandem repeat proteins with longer repeat topologies and enhanced subunit contact surfaces.
Commun Biol, 4:1240-1240, 2021

PubMed Abstract: Circular tandem repeat proteins ('cTRPs') are de novo designed protein scaffolds (in this and prior studies, based on antiparallel two-helix bundles) that contain repeated protein sequences and structural motifs and form closed circular structures. They can display significant stability and solubility, a wide range of sizes, and are useful as protein display particles for biotechnology applications. However, cTRPs also demonstrate inefficient self-assembly from smaller subunits. In this study, we describe a new generation of cTRPs, with longer repeats and increased interaction surfaces, which enhanced the self-assembly of two significantly different sizes of homotrimeric constructs. Finally, we demonstrated functionalization of these constructs with (1) a hexameric array of peptide-binding SH2 domains, and (2) a trimeric array of anti-SARS CoV-2 VHH domains. The latter proved capable of sub-nanomolar binding affinities towards the viral receptor binding domain and potent viral neutralization function.

PubMed: 34716407
DOI: 10.1038/s42003-021-02766-y

実験手法

X-RAY DIFFRACTION (3.2 Å)