Journal: RSC Advances

Article Title: Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design †

doi: 10.1039/d1ra01173a

Figure Lengend Snippet: Overview of the T2R-TTL-ligand complex structure and the chemical structures of the bound ligands. (A) Overall structure of the tubulin–ELR510444 complex. RB3-SLD is shown in yellow, TTL in blue, α-tubulin in green, β-tubulin in pink, GTP in red, GDP in grey, and ELR510444 in cyan. GTP, GDP, and ELR510444 are shown as spheres. (B) Chemical structure of ELR510444. (C) Experimental electron density map (Fo–Fc) contoured at 2.0 σ around ELR510444. (D) Chemical structure of parbendazole. (E) The electron densities of parbendazole. The Fo–Fc omit map is shown in grey and contoured at 1.5 σ .

Article Snippet: ELR510444 and parbendazole were purchased from MedChem Express.

Techniques:

Journal: RSC Advances

Article Title: Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design †

doi: 10.1039/d1ra01173a

Figure Lengend Snippet: Data collection and refinement statistics for X-ray structures a

Article Snippet: ELR510444 and parbendazole were purchased from MedChem Express.

Techniques:

Journal: RSC Advances

Article Title: Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design †

doi: 10.1039/d1ra01173a

Figure Lengend Snippet: Detailed interactions of ELR510444 with tubulin. Surface view of the ELR510444–tubulin complex (A) and intermolecular interactions of the binding (B). (C) Two-dimensional interaction map of the ELR510444 complex with β-tubulin.

Article Snippet: ELR510444 and parbendazole were purchased from MedChem Express.

Techniques: Binding Assay

Journal: RSC Advances

Article Title: Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design †

doi: 10.1039/d1ra01173a

Figure Lengend Snippet: Comparison of the binding modes of ELR510444, parbendazole, and colchicine. (A) Chemical structure of colchicine. (B) Superimposition of β-tubulin binding with ELR510444 (cyan sticks), parbendazole (yellow sticks), and colchicine (grey sticks) in CBS. (C) Conformation of the αT5 and βT7 loops differs significantly when ELR510444 or colchicine is bound. (D) Superimposition of parbendazole and colchicine. Residues with significant differences in conformation are highlighted with 2Fo–Fc map contours.

Article Snippet: ELR510444 and parbendazole were purchased from MedChem Express.

Techniques: Comparison, Binding Assay

Journal: RSC Advances

Article Title: Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design †

doi: 10.1039/d1ra01173a

Figure Lengend Snippet: Alignment of ELR510444 and C22. ELR510444 (cyan sticks) was copied from the crystal structure, whereas C22 (magenta sticks) was docked into the CBS by Autodock Vina. Interactions between C22 and β-tubulin differing from that of ELR510444 are highlighted by yellow dashed lines.

Article Snippet: ELR510444 and parbendazole were purchased from MedChem Express.

Techniques:

Journal: RSC Advances

Article Title: Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design †

doi: 10.1039/d1ra01173a

Figure Lengend Snippet: Predicted binding affinities of designed compounds

Article Snippet: ELR510444 and parbendazole were purchased from MedChem Express.

Techniques: Binding Assay