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-Structure paper
| タイトル | Design of functionalised circular tandem repeat proteins with longer repeat topologies and enhanced subunit contact surfaces. |
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| ジャーナル・号・ページ | Commun Biol, Vol. 4, Issue 1, Page 1240, Year 2021 |
| 掲載日 | 2021年10月29日 |
著者 | Jazmine P Hallinan / Lindsey A Doyle / Betty W Shen / Mesfin M Gewe / Brittany Takushi / Madison A Kennedy / Della Friend / James M Roberts / Philip Bradley / Barry L Stoddard / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Commun Biol / PubMed:34716407 / PubMed Central |
| 手法 | EM (単粒子) / X線回折 |
| 解像度 | 2.1 - 6.5 Å |
| 構造データ | EMDB-24425, PDB-7rdr: ![]() PDB-6xr1: ![]() PDB-6xr2: |
| 化合物 | ![]() ChemComp-HOH: |
| 由来 |
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キーワード | DE NOVO PROTEIN / Computationally designed / de novo / toroid / helix-turn-helix / PEPTIDE BINDING PROTEIN / protein display particles |
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