Alpha-2B adrenergic receptor

Alpha-2B adrenergic receptor

Adrenoceptor alpha 2B
Available structures
PDB Ortholog search: RCSB

The alpha-2B adrenergic receptor2B adrenoceptor), is a G-protein coupled receptor. It is a subtype of the adrenergic receptor family. The human gene encoding this receptor has the symbol ADRA2B.[1] ADRA2B orthologs[2] have been identified in several mammals.


Alpha-2-adrenergic receptors include 3 highly homologous subtypes: alpha2A, alpha2B, and alpha2C. These receptors have a critical role in regulating neurotransmitter release from sympathetic nerves and from adrenergic neurons in the central nervous system.


This gene encodes the alpha2B subtype, which was observed to associate with eIF-2B, a guanine nucleotide exchange protein that functions in regulation of translation. A polymorphic variant of the alpha2B subtype, which lacks 3 glutamic acids from a glutamic acid repeat element, was identified to have decreased G protein-coupled receptor kinase-mediated phosphorylation and desensitization; this polymorphic form is also associated with reduced basal metabolic rate in obese subjects and may therefore contribute to the pathogenesis of obesity. This gene contains no introns in either its coding or untranslated sequences.[1]

A deletion variant of the alpha-2B adrenergic receptor has been shown to be related to emotional memory in Europeans and Africans.[3]

In October 2013 researchers from the University of British Columbia confirmed this and further reported that the variant predisposed those people who had it to focus more on negative aspects of a situation. Prof. Rebecca Todd claimed "This is the first study to find that this genetic variation can significantly affect how people see and experience the world.”


The ADRA2B gene (sometimes referenced as A2AB) is used in animals as a nuclear DNA phylogenetic marker.[2] This intronless gene has first been used to explore the phylogeny of the major groups of mammals,[4] and contributed to reveal that placental orders are distributed into four major clades: Xenarthra, Afrotheria, Laurasiatheria, and Euarchonta plus Glires. Comparative analysis of the primary protein sequence of ADRA2B across placentals also showed the high conservation of residues thought to be involved in agonist binding and in G protein–coupling. However, great variations are observed in the very long, third intracellular loop, with a polyglutamyl domain displaying pervasive length differences.[5]

Selective Ligands


See also


Further reading

External links