G-protein Coupled Receptor: Difference between revisions

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= Structure  =
= Structure  =


Along with the seven transmembrane core structure, the G Protein Coupled Receptor often have large receptor domains in the N-terminus on the extracellular side of the plasma membrane. Binding of a signal molecule to this receptor domain (or indeed the extracellular part of the transmembrane domains) cause a conformational change in the transmembrane domain and intracellular C-terminus. This triggers the action of a [[G-proteins|G-protein]] which binds guanyl nucleotides. <ref>Berg, JM, Biochemistry, 6th Edition (2007), WH Freeman and Company, New York</ref>(Berg, J.M., Stryer)
Along with the seven transmembrane core structure, the G Protein Coupled Receptor often have large receptor domains in the N-terminus on the extracellular side of the plasma membrane. Binding of a signal molecule to this receptor domain (or indeed the extracellular part of the transmembrane domains) cause a conformational change in the transmembrane domain and intracellular C-terminus. This triggers the action of a [[G-proteins|G-protein]] which binds guanyl nucleotides. <ref>Berg, JM, Biochemistry, 6th Edition (2007), WH Freeman and Company, New York</ref>


= References  =
= References  =


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<references />&nbsp;

Revision as of 15:46, 16 November 2010

The G-protein-coupled receptor (GPCR) is a seven transmembrane spanning receptor that interacts with G-protein in the process of cell signalling. It constitutes along with ion-channel-coupled receptors and enzyme-coupled receptors a major class of cell surface-receptor[1].

Classification

Over 800 G-protein-coupled receptors have been identified (more than half of them being olfactory receptors) and phylogenetic studies carried out[2]. From these studies the GPCRs can be classified in five main families: 

Structure

Along with the seven transmembrane core structure, the G Protein Coupled Receptor often have large receptor domains in the N-terminus on the extracellular side of the plasma membrane. Binding of a signal molecule to this receptor domain (or indeed the extracellular part of the transmembrane domains) cause a conformational change in the transmembrane domain and intracellular C-terminus. This triggers the action of a G-protein which binds guanyl nucleotides. [3]

References

  1. Alberts, et al. Molecular Biology of the Cell. 5th ed. Garland Science. 2008
  2. Fredriksson R, Lagerström MC, Lundin LG, Schiöth HB. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints.Mol Pharmacol. 2003 Jun;63(6):1256-72.
  3. Berg, JM, Biochemistry, 6th Edition (2007), WH Freeman and Company, New York