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J Cell Mol Med. 2007 Sep-Oct;11(5):908-22.

Structure and function of the human calcium-sensing receptor: insights from natural and engineered mutations and allosteric modulators.

Author information

1
Molecular Signalling Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. jianxinh@niddk.nih.gov

Abstract

The human extracellular Ca(2+)-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 orthosteric 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.

PMID:
17979873
PMCID:
PMC4401263
DOI:
10.1111/j.1582-4934.2007.00096.x
[Indexed for MEDLINE]
Free PMC Article

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