LA JOLLA, CA July 12, 2012 Readers of the top-ranked scientific journals Science and Nature might have noticed a recent wave of articles, most recently in the July 13, 2012 issue of Science, with deep importance for biology and medicine. These papers, all published this year by collaborations headed by the Scripps Research Institute laboratory of Professor Raymond Stevens, illuminate a large and medically important family of proteins called G protein-coupled receptors (GPCRs).
GPCRs sit in the cell membrane and sense various molecules outside the cell, including odors, hormones, neurotransmitters, and light. After binding these molecules, GPCRs trigger a specific response inside the cell. Many drugs, including allergy and heart medication and drugs for Parkinson's and Huntington's disease, target these proteins.
This year, a paper published January 19 (Liu et al., Science, 335, 1106) was quickly followed by related publications on the crystal structures of a lipid GPCR (Hanson et al., Science, 335, 851, February 17), the kappa opioid receptor (Wu et al., Nature, 485, 327, March 21), and the nociceptin opioid receptor (Thompson et al., Nature, 485, 395, May 17). The most recent publication is on the 1.8 angstrom high-resolution structure of the A2A adenosine receptor (Liu et al., Science, 336, 232, July 13) and is one of the highest resolution structures to date of a human membrane protein. The structure highlights the receptor and ligand as an allosteric machine controlled by sodium, water, cholesterol, and lipids.
These findings were made possible by technologies developed by the NIH Common Fund Joint Center for Innovative Membrane Technologies (JCIMPT) and the biological questions pursued by the GPCR Network, part of the Protein Structure Initiative:Biology at the National Institute for General Medical Sciences (NIGMS) in Bethesda, Maryland (NIGMS PSI:Biology).
|Contact: Mika Ono|
Scripps Research Institute