Cell signal transduction: hormones, neurotransmitters and therapeutic drugs relate to purine nucleotide structure

• Published in: Journal of receptors and signal transduction Vol. 38; no. 2; p. 101
• Main Author: Williams, W R
• Format: Journal Article
• Language: English
• Published: England 01.04.2018
• Subjects: Adenosine Triphosphate - chemistry; Adenosine Triphosphate - metabolism; Animals; Cells - metabolism; GTP-Binding Proteins - chemistry; GTP-Binding Proteins - metabolism; Hormones - metabolism; Ligands; Models, Molecular; Neurotransmitter Agents - metabolism; Pharmaceutical Preparations - metabolism; Protein Subunits - chemistry; Protein Subunits - metabolism; Purine Nucleotides - chemistry; Purine Nucleotides - metabolism; Signal Transduction; Molecular structure; purine nucleotides; signal transduction
• ISSN: 1532-4281
• DOI: 10.1080/10799893.2018.1431279

Purine nucleotides transduce cell membrane receptor responses and modulate ion channel activity. This is accomplished through conformational change in the structure of nucleotides and cell membrane associated proteins. The aim of this study is to enhance our understanding of nucleotide dependence in regard to signal transduction events, drug action and pharmacological promiscuity. Nucleotides and ligand structures regulating Gα protein subunits, voltage- and ligand-gated ion channels are investigated for molecular similarity using a computational program. Results differentiate agonist and antagonist structures, identify molecular similarity within nucleotide and ligand structures and demonstrate the potential of ligands to regulate nucleotide conformational change. Relative molecular similarity within nucleotides and the ligands of the major receptor classes provides insight into mechanisms of receptor and ion channel regulation. The nucleotide template model has some merit as an initial screening tool in the study and comparison of drug and hormone structures.