Optimal 1TEL–target protein linker character is target protein-dependent

Pedroza Romo, M.J.; Keliiliki, A.; Averett, J.C.; Gonzalez, J.F.; Noakes, E.; Wilson, E.W.; Smith, C.; Averett, B.; Hansen, D.; Nickles, R.; Bradford, M.; Soleimani, S.; Smith, T.; Nawarathnage, S.; Samarwickrama, P.; Kelsch, A.; Bunn, D.; Stewart, C.; Abiodun, W.; Tsubaki, E.; Brown, S.; Doukov, T.I.; Moody, J.D.

doi:10.1107/S2059798326002494

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 4
Structure and lattice interactions of a `2-fold' 1TEL-short-rigid-DARPin crystal. (a) Structure of the `2-fold' 1TEL-short-rigid-DARPin monomer (PDB entry 9dvg), with 1TEL shown in pale pink and DARPin in magenta. (b) The unit cell of 1TEL-short-rigid-DARPin in space group P6₅ is outlined in black, with symmetry mates displayed in the same colouring as in (a). (c) Crystal lattice representation with 1TEL polymers shown as ribbons and symmetry mates displayed in grey. 1TEL regions are in light grey, DARPin regions are in dark grey and the monomer is coloured as in (a). (d) Close-up view of the interaction between two DARPins, with interacting residues shown as sticks and spheres. (e, f) Two unique interactions between the DARPin (magenta) and nearby 1TELs (light grey) from the host polymer or a neighbouring polymer. Figures were prepared using PyMOL (Schrödinger) and Microsoft PowerPoint.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 82| Part 5| May 2026| Pages 516-532

https://doi.org/10.1107/S2059798326002494

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