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TitleDesign of functionalised circular tandem repeat proteins with longer repeat topologies and enhanced subunit contact surfaces.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 1240, Year 2021
Publish dateOct 29, 2021
AuthorsJazmine 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 AbstractCircular 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.
External linksCommun Biol / PubMed:34716407 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.1 - 6.5 Å
Structure data

24425

7rdr

EMDB-24425, PDB-7rdr:
Circular tandem repeat protein with novel repeat topology and enhanced subunit contact surfaces
Method: EM (single particle) / Resolution: 6.5 Å

PDB-6xr1:
Computationally designed right-handed alpha/alpha single-chain toroid with 9 repeats
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6xr2:
Computationally designed right-handed alpha/alpha homotrimeric toroid with 3 repeats per subunit
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • unidentified (others)
  • synthetic construct (others)
KeywordsDE NOVO PROTEIN / Computationally designed / de novo / toroid / helix-turn-helix / PEPTIDE BINDING PROTEIN / protein display particles

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