Fig. 3: The different β5 register shifts observed in the 7B8-bound structure of Af2. | Communications Biology

Fig. 3: The different β5 register shifts observed in the 7B8-bound structure of Af2.

From: Ubiquitin-derived artificial binding proteins targeting oncofetal fibronectin reveal scaffold plasticity by β-strand slippage

Fig. 3

a Overall structure of 7B8-bound Af2 depicting the distribution of the evolved residues of Ub-N and Ub-C (side chains shown as lines, C-atoms of Ub-N cyan, C-atoms of Ub-C magenta). Linker residues coloured in green. The β5 strands of Af2 Ubi-N (darker blue) and Ubi-C (darker red) exhibit distinct negative register shifts, extending the α2β5 loops involved in target binding. Structural superposition of Ub-wt (PDB id 1UBQ, light grey, black labels) and (b) the Ub-N domain of Af2 (light blue, blue labels, evolved residues shown in cyan) revealing the -2 register-shift of β5 (darker blue) and (c) the Ub-C domain of Af2 (light red, red labels with asterisk, corresponding to residue numbering of Ub-N domain, evolved residues shown in magenta) exhibiting a -4 register-shift of β5 (darker red). Af2 residues relocated by the β5 register shifts and corresponding residues of Ub-wt shown as sticks.

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