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Adenosine deaminase (ADA) perpetuates chronic inflammation by degrading extracellular adenosine which is toxic for lymphocytes. ADA has two distinct conformations: open form and closed form [1]. From the crystal structures with various ligands, the non-nucleoside type inhibitors bind to the active site occupying the critical water-binding position and sustain the open form of apo-ADA. In contrast, substrate mimics do not occupy the critical position, and induce the large conformational change to the closed form. However, it is difficult to predict the binding of (+)-erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), as it possesses characteristic parts of both the substrate and the non-nucleoside inhibitors. The crystal structure shows that EHNA binds to the open form through a novel recognition of the adenine base accompanying conformational change from the closed form of the PRADA complex in crystalline state [2]. The open form crystal structure of the EHNA-ADA complex supports our hypothesis that the occupancy at the trigger-water-position is critical for determining the open/closed conformational alternation, rather than the nucleoside framework binding. We believe that the structural penetration of the EHNAADA complex and structural comparison of the other inhibitor-ADA complexes will support the discovery of novel ADA inhibitors by structure-based drug design.

The structure of the Ca2+-ATPase bound to cyclopiazonic acid reveals a complexed divalent ion

The structure of the Ca²⁺-ATPase bound to cyclopiazonic acid reveals a complexed divalent ion