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A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for ribosyl-modified
and unmodified nucleotide inhibitors

URN to cite this document:
urn:nbn:de:bvb:355-epub-26664
Wang, Jenna L. ; Guo, Jian-Xin ; Zhang, Qi-Yuan ; Wu, Jay J.-Q. ; Seifert, Roland ; Lushington, Gerald H.
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Date of publication of this fulltext: 05 Aug 2009 13:40


Abstract

Abstract—Adenylyl cyclases (ACs) are promising pharmacological targets for treating heart failure, cancer, and psychosis. Ribosesubstituted 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 pKi values. Energy ...

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