 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](mh5164fig2mag.jpg)
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Figure 2
Overall structure and molecular interactions between Pals1PDZ and Crb17. (a) Difference electron density (green) for the Crb17 peptide bound to Pals1PDZ prior to fitting. The map is a σA-weighted Fo − Fc electron-density OMIT map (contoured at σ = 3.0). (b) Electron density for the Crb17 peptide bound to Pals1PDZ after refinement. The map is shown as a σA-weighted 2Fo − Fc electron-density OMIT map (contoured at σ = 1.0). (c) Schematic representation of Crb17 (green) bound to Pals1PDZ (grey cartoon). Secondary-structure elements are labelled starting from the N-terminus of Pals1PDZ. α, α-Helix; β, β-strand. (d) Close-up of the Crb17 peptide (green sticks) bound to Pals1PDZ (grey cartoon). Pals1 residues involved in the recognition of Crumbs are shown as sticks. Pink dashed lines represent hydrogen bonds that are established between the Crb17 peptide and Pals1PDZ. |
![[Figure 2]](mh5164fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
