Structures of designed armadillo-repeat proteins show propagation of inter-repeat interface effects

Reichen, C.; Madhurantakam, C.; Hansen, S.; Grütter, M.G.; Plückthun, A.; Mittl, P.R.E.

doi:10.1107/S2059798315023116

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Interface between internal repeats M₃ and M₄ in chain C of His-Y_IIIM₄A_II (a) and His-Y_IIIM₅A_II (b). The dArmRPs are shown in blue and grey and the His₆ tag with salmon C atoms. (c) Superposition based on the N-cap and internal repeats M₁–M₃ of His-Y_IIIM₅A_II chain A (dark blue), His-Y_IIIM₅A_II chain C (light blue) and Y_IIIM₅A_II (orange). Residues at the M₃–M₄ interface are labelled. (d) C^α trace of Y_IIIM₅A_II coloured in green (N-cap), blue (internal repeats) and orange (C-cap). The Leu³², Trp³³ and Thr³⁴ side chains are shown as sticks in blue, grey and green, respectively. Hydrogen bonds and general distances are shown as orange and grey dotted lines, respectively. Distances and conformations of Leu³² side chains are indicated (tg⁺, trans/gauche⁺; g⁻t, gauche⁻/trans).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 72| Part 1| January 2016| Pages 168-175

https://doi.org/10.1107/S2059798315023116

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