1. The Intersection of Structural and Chemical Biology - An Essential Synergy 
William J. Zuercher, Jonathan M. Elkins, Stefan Knapp 
Cell Chemical Biology 
Volume 23, Issue 1, Pages (January 2016)
DOI: /j.chembiol
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2. Figure 1 Structural Plasticity of Aurora Kinase A
(A) Structural superimposition of 5 Aurora A structures (PDB code: 5AAD [magenta, imidazopyrimidine complex]; PDB code: 4UTD [red; AMP-PCP]; PDB code: 4UYN [gray; pyrroloquinoline SAR156497]; PDB code: 4B0G [green, imidazopyrimidine]; 4DEA [blue, pyrimidine-diyldiimino dibezoic acid]). The main structural elements are labeled and the ATP binding site shown in detail in (B) is boxed.
(B) Structural changes in the ATP binding site. An AMP-PCP molecule is also shown in ball-and-stick representation to highlight the location of the ATP binding site.
(C) Detailed comparison of two structures: the complex with the non-hydrolyzable ATP analog AMP-PCP (PDB code: 4UTD) and an imidazopyrimidine complex (PDB code: 4B0G).
Cell Chemical Biology  , DOI: ( /j.chembiol )
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3. Figure 2
Chemical Probes Developed for Bromodomains and Coverage of This Family of Protein Interaction Domains by Crystal Structures
Available crystal structures for each domain in the structure-based phylogenetic tree are indicated by a blue triangle. Chemical probe names and targeted bromodomains are indicated. Many more inhibitors have been reported for BET bromodomains, which have not been included due to space limitations.
Cell Chemical Biology  , DOI: ( /j.chembiol )
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4. Figure 3 Generation of a Bromodomain Targeted Fragment Library
The figure describes the approached used by Vidler et al. (2013). Potential acetyl-lysine mimetic fragments were extracted from known inhibitors or were derived by similarity searching. Diversification of the fragments was enhanced by potential bioisosteric replacements. Searching public databases of commercial compounds resulted in the identification of potential inhibitors containing the fragment. Docking suggested the most likely inhibitors that were purchased and screened against the target and other bromodomains. Subsequent structure determination confirmed the docking pose and provided a model for lead expansion.
Cell Chemical Biology  , DOI: ( /j.chembiol )
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5. Figure 4
Development of MDM2-p53 Interaction Inhibitors Using the W23 Anchor Residue
Structure of MDM2 in complex with a stabilized p53 peptide (PDB code: 3V3B). The MDM2 binding pocket is shown as a solid surface. Three key p53 residues are shown in ball-and-stick representation. Potent lead compounds using an oxindole bioisostere were used in a pharmacophore search that identified natural products such as spiro-tryprostatin A. Optimization of the central spiro-oxindole core structure using structure-based design resulted in potent compounds that were further optimized to clinical inhibitors that target the p53-MDM2 interaction.
Cell Chemical Biology  , DOI: ( /j.chembiol )
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