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 3
Structure and lattice interactions of a 1TEL-medium-rigid-DARPin crystal. (a) Structure of the 10×His-1TEL-medium-rigid-DARPin monomer (PDB entry 9dp8), with 1TEL shown in pale cyan, the medium-rigid linker in black and DARPin in bright cyan. (b) The unit cell of 10×His-1TEL-medium-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 pastel cyan and light grey, DARPin regions are dark grey and the monomer is coloured as in (a). (d) Close-up view of the interaction between the DARPin (bright cyan) and the 1TEL unit one helical turn below it (light grey). Proteins are depicted in cartoon representation, with interacting residues shown as sticks and spheres. (e) As in (d), but showing interactions between the DARPin (bright cyan) and the adjacent DARPin from 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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