Structural and biochemical insights into purine-based drug molecules in hBRD2 delineate a unique binding mode opening new vistas in the design of inhibitors of the BET family

Arole, A.H.; Deshmukh, P.; Sridhar, A.; Mathur, S.; Mahalingaswamy, M.; Subramanya, H.; Dalavaikodihalli Nanjaiah, N.; Padmanabhan, B.

doi:10.1107/S2059798323005211

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 6
The crystal structures of BRD2 bromodomains in complex with AC2. (a) Polder difference Fourier map of AC2 in complex with BD1 at site 1 contoured at 3σ and at site 2 contoured at 2.7σ. A closer view of the intermolecular interactions established by AC2 at site 1 (right) and site 2 (left) is shown. (b) Polder difference Fourier map of AC2 in complex with BD2 at site 1 contoured at 2.7σ. The AC2 molecule possesses alternate conformations: a closer view of the intermolecular interactions established by AC2 at site 1 is shown (right).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 79| Part 8| August 2023| Pages 758-774

https://doi.org/10.1107/S2059798323005211

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