 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](no5185fig1mag.jpg)
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Figure 1
Details of the HER3d4–DARPin D5 complex. (a) Superposition of the HER3d4–DARPin D5 complexes in the orthorhombic (gray) and monoclinic (magenta) settings. Molecules within the same ab layer are shown as molecular surfaces in gray. The unit-cell c axis in the orthorhombic setting is shown as an orange dotted line. (b) Overview of the complex. The DARPin D5 N-cap, internal repeats 1 and 2 and the C-cap are shown as cartoons in green, dark blue, light blue and orange, respectively. HER3d4 furin-like domains 1–3 are colored pink, gray and cyan. Cysteines are shown as green sticks. The protruding loop is highlighted in red (residues 571–584). (c) Superposition of the furin-like cysteine-rich domains of HER3d4. Coloring is as in (b). The N- and C-termini are labeled in bold. Disulfide bridges (A–D) are labeled in italics. (d) The 2mFo − DFc electron-density map for HER3d4 residues 571–576 was contoured at 1.2σ. (e) Details of the DARPin D5–HER3d4 interface. HER3 residues are shown with gray C atoms and chain breaks are highlighted by spheres. Residues at randomized DARPin positions and the framework residues Leu53 and Gln86 are shown as blue sticks, hydrogen bonds as yellow dashed lines and water molecules as red spheres. |
![[Figure 1]](no5185fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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