Editor's Summary

15 November 2007

A tough structure to crack

Most hormones and neurotransmitters — and therefore many drugs — work via G protein-coupled receptors, or GPCRs. With the one exception of rhodopsin, the most stable GPCR known, structural data for these proteins are hard to come by. Now several collaborating research groups, publishing in this issue of Nature and also in Science, have exploited a raft of different techniques, including the use of the inverse agonist carazolol to stabilize the receptor structure, to determine the crystal structure of the human beta2AR adrenaline receptor. Its structure contrasts markedly with that of 'dark' rhodopsin, which helps explain why it is so hard to prepare diffraction-quality crystals of most GPCRs.

News and ViewsStructural biology: A receptor unlocked

G-protein-coupled receptors govern many biological functions, yet little is known about the molecular basis of their activity. The structure of a prominent example of these receptors is now revealed.

Stephen R. Sprang


ArticleCrystal structure of the human bold beta2 adrenergic G-protein-coupled receptor

Søren G. F. Rasmussen, Hee-Jung Choi, Daniel M. Rosenbaum, Tong Sun Kobilka, Foon Sun Thian, Patricia C. Edwards, Manfred Burghammer, Venkata R. P. Ratnala, Ruslan Sanishvili, Robert F. Fischetti, Gebhard F. X. Schertler, William I. Weis & Brian K. Kobilka