 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 5]](dz5101fig5mag.jpg)
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Figure 5
Two models for the binding of a peptide into the crystal structure of CD59. (a) Docking of the peptide comprising residues VSLAFS into the crystal structure by superimposition of the NMR-derived model of CD59 with the crystal structure. (b) The same view, but now showing how a loop from a symmetry-related molecule of CD59, comprising residues 20–24, binds into the same region of CD59. In both cases, CD59 is shown in stick form and is covered by a transparent surface. Residues and their respective surfaces that are within contact range of each peptide are colored blue. The remaining residues and surface of CD59 are both colored brown. Each `peptide' is shown in stick form and is colored yellow. Residues involved in contacts are labeled using single-letter code for the peptide and residue number for the crystal-packing interaction (#, symmetry-related residue). This figure was produced with PyMOL (https://www.pymol.org ). |
![[Figure 5]](dz5101fig5.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
