Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins

Biology Direct

Daria N. Shalaeva¹  Michael Y. Galperin²  Armen Y. Mulkidjanian³ 

[1] School of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119992, Russia

[2] National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda 20894, MD, USA

[3] A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119992, Russia

关键词: Chemoreceptor;    Signal transduction;    Evolution;    GPCR;    Opioid receptor;    Proteorhodopsin;    Sensory rhodopsin;    Halorhodopsin;    Bacteriorhodopsin;    Vision;   

Others  :  1230609
DOI  :  10.1186/s13062-015-0091-4

 received in 2015-07-07, accepted in 2015-10-12,  发布年份 2015

【 摘 要 】

Microbial rhodopsins and G-protein coupled receptors (GPCRs, which include animal rhodopsins) are two distinct (super) families of heptahelical (7TM) membrane proteins that share obvious structural similarities but no significant sequence similarity. Comparison of the recently solved high-resolution structures of the sodium-translocating bacterial rhodopsin and various Na ⁺ -binding GPCRs revealed striking similarity of their sodium-binding sites. This similarity allowed us to construct a structure-guided sequence alignment for the two (super)families, which highlighted their evolutionary relatedness. Our analysis supports a common underlying molecular mechanism for both families that involves a highly conserved aromatic residue playing a pivotal role in rotation of the 6th transmembrane helix.

【 授权许可】

   
2015 Shalaeva et al.

【 图 表 】

Fig. 1.

Fig. 2.

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