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  • 标题:Common and distinct mechanisms of activation of rhodopsin and other G protein-coupled receptors
  • 本地全文:下载
  • 作者:Sumire Nakamura ; Takeshi Itabashi ; Daisuke Ogawa
  • 期刊名称:Scientific Reports
  • 电子版ISSN:2045-2322
  • 出版年度:2013
  • 卷号:3
  • DOI:10.1038/srep01844
  • 出版社:Springer Nature
  • 摘要:Detailed and systematic examination of high-resolution structural data is a rational strategy for understanding the function of biological macromolecules. G protein-coupled receptors (GPCRs) are an exceptionally valuable superfamily of proteins for such analysis. The most intriguing question is how a variety of extracellular stimuli evoke structural changes in the intracellular surface of the receptors. The recent active-like crystal structures of GPCRs provide information for uncovering common and distinct mechanisms of light-induced and ligand-induced activation. Based on systematic structural alignment, we have analyzed 3 receptors (rhodopsin, β2 adrenergic receptor, adenosine A2A receptor) and demonstrate that the extracellular movement of helix VI is significantly different between rhodopsin and the other 2 receptors, and that the extracellular side of helix III exhibits distinct features in the 3 receptors. These findings not only emphasize the specialization of rhodopsin as a photoreceptor but also provide insights into the mechanism leading to rearrangement of helix VI.
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