 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](mv5092fig4mag.jpg)
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Figure 4
The relative positions of Glu84 and Arg86 of CaM and an arginine from a ligand peptide. (a) When swinging in to interact with the backbone, the two residues in the two crystal forms reach towards the same position: the helical groove between residues 79–80 and 83–84. (b) The complex between CaM and a peptide from DAP kinase (de Diego et al., 2010  ; PDB entry 1yr5
) shows an interaction between the backbone of the disrupted helix, including Thr79, and the side chain of Arg317 from the peptide. A salt bridge is also present between Glu84 and this arginine residue, while Arg86 is far away from the peptide and in fact interacts with Tyr138. (c) A comparison between the bent conformation (grey; central linker in orange) and the fully collapsed peptide complex (green; central linker in pink) shows that the bending region corresponds to that required for complex formation. In both structures, an arginine residue interacts with the unfolded central helix backbone. |
![[Figure 4]](mv5092fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
