Structure and function of the human calcium-sensing receptor: insights from natural and engineered mutations and allosteric modulators.
Hu, Jianxin a; Spiegel, Allen M. b
[Review]
Journal of Cellular & Molecular Medicine.
11(5):908-922, September/October 2007.
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The human extracellular Ca2 -sensing receptor (CaR), a member of the G protein-coupled receptor family 3, plays a key role in the regulation of extracellular calcium homeostasis. It is one of just a few G protein-coupled receptors with a large number of naturally occurring mutations identified in patients. In contrast to the small sizes of its agonists, this large dimeric receptor consists of domains with topologically distinctive orthos-teric and allosteric sites. Information derived from studies of naturally occurring mutations, engineered mutations, allosteric modulators and crystal structures of the agonist-binding domain of homologous type 1 metabotropic glutamate receptor and G protein-coupled rhodopsin offers new insights into the structure and function of the CaR.
Copyright (C) 2007 Blackwell Publishing Ltd.