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 1
Structural and lattice interactions of 3TEL-GGG-DARPin. (a) Structure of the 3TEL-GGG-DARPin monomer (PDB entry 9e4q), with 3TEL shown in pale orange and DARPin in bright orange. (b) The 3TEL-GGG-DARPin unit cell (space group P2₁2₁2₁) is outlined in black, with symmetry mates displayed in the same colouring as in (a). (c) Crystal lattice contacts in this crystal, with 3TEL polymers shown as ribbons and symmetry mates displayed in grey. 3TEL regions are in light grey, DARPin regions are in dark grey and the monomer is coloured as in (a). (d) The DARPin docked configuration from the 3TEL-GGG-DARPin structure superimposed onto successive 1TEL subunits of a 1TEL polymer. Neighbouring DARPins are coloured orange and blue. (e) As in (d), but for one helical turn of the canonical 1TEL P6₅ 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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