journal menu
![[Figure 5]](jb5013fig5mag.jpg)
|
|
Figure 5
An overlay showing the displacement of the Mcl-1 BH3 helix by a symmetry-related copy of the C-terminal scFv tag remnant. (a) Overview of the crystal contact between a symmetry-related molecule, shown as a Cα trace, and the BH3 binding pocket of Mcl-1, shown as a surface. By chance, the tag remnant is positioned such that it is able to make an ordered interaction with the pocket. (b) A more detailed view of the interaction between the scFv tag remnant and the BH3 pocket of Mcl-1. The tag remnant is shown as an orange Cα trace with side chains as sticks, and the BH3 binding site of Mcl-1 is shown as a white cartoon with side chains as sticks. The apo Mcl-1–scFv complex (PDB entry 6qb3) is overlaid in rose, showing the binding effect on the BH3 binding groove. Although there is a considerable displacement and conformational rearrangement of the helix, the Sδ atom of Met250 remains in approximately the same place (highlighted with an asterisk), demonstrating the plasticity of the ligand-binding pocket. The interactions are mostly hydrophobic, but a hydrogen bond (2.8 Å) was observed between His224 of Mcl-1 and Glu250 of the scFv (dashed line). |
![[Figure 5]](jb5013fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
