Wang, Jenna L. and Guo, Jian-Xin and Zhang, Qi-Yuan and Wu, Jay J. -Q. and Seifert, Roland and Lushington, Gerald H. (2007) A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for ribosyl-modified and unmodified nucleotide inhibitors. BIOORGANIC & MEDICINAL CHEMISTRY, 15 (8). pp. 2993-3002. ISSN 0968-0896,
Full text not available from this repository. (Request a copy)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. (c) 2007 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | FORCE-FIELD; PROTEINS; MECHANISM; ANALOGS; PURINE; GTP; adenylyl cyclase; conformational transition; molecular modeling; MANT-substituted nucleotides |
| Subjects: | 600 Technology > 615 Pharmacy |
| Divisions: | Chemistry and Pharmacy > Institute of Pharmacy > Pharmacology and Toxicology (Prof. Schlossmann, formerly Prof. Seifert) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Dec 2020 11:36 |
| Last Modified: | 14 Dec 2020 11:36 |
| URI: | https://pred.uni-regensburg.de/id/eprint/32881 |
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