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Updated: Jul 16, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
Published on: October 8, 2015
A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for
Jenna L Wang1, Jian-Xin Guo, Qi-Yuan Zhang
1Molecular Graphics and Modeling Laboratory, University of Kansas, Lawrence, KS 66045, USA.
Abstract:
Adenylyl cyclases (ACs) are promising pharmacological targets for treating heart failure, cancer, and psychosis. Ribose-substituted nucleotides have been reported as a potent family of AC inhibitors. In silico analysis of the docked conformers of such nucleotides in AC permits assembly of a consistent, intuitive QSAR model with strong correlation relative to measured pK(i) values. Energy decomposition suggests that the MANT group effects an AC conformational transition upon ligand binding.
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