Adenylate cyclases (ACs) are the membrane-bound glycoproteins that convert ATP to cAMP and pyrophosphate.
When activated by G-protein Gs, adenylate cyclases (ACs), which are membrane-bound glycoproteins, catalyze the synthesis of cAMP from ATP.
Different AC isoforms are widely expressed in various tissues that participate in regulatory systems in response to particular stimuli.
Humans have 9 different AC isoforms, with AC5 and AC6 thought to be particularly important for cardiac activities.
Nitric oxide has an impact on the activity of AC6, hence the protein's nitrosylation may control how it works. However, little is known about the structural variables that affect nitrosylation in ACs and how they relate to G's.
We predict the cysteines that are prone to nitrosylation using this 3D model, and we use virtual ligand screening to find potential new AC6 ligands.
According to our model, the AC-Gs interface's Cys174 in G's and Cys1004 in AC6 (subunit C2) are two potential residues that could experience reversible nitrosylation.
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