FIGURE 2. Structure of the bold beta2AR365–Fab5 complex.

From the following article:

Crystal structure of the human 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

Nature 450, 383-387(15 November 2007)

doi:10.1038/nature06325

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a, Packing of the beta2AR365–Fab5 complex in crystals formed in DMPC bicelles (beta2AR, gold; heavy chain, blue; light chain, red). b, Structure of the beta2AR showing sites of the interactions with Fab5. Sites of specific (idiotypic) interactions between Fab5 and the beta2AR are shown in green. Sites of interactions between the beta2AR and the constant region of Fab5 of the symmetry mate are shown in magenta. Dotted grey lines indicate predicted membrane boundaries. Solid black lines indicate extracellular connections between transmembrane segments. c, FO–FC map contoured at 2.0 sigma and surrounded by residues known to be involved in ligand binding. The chemical structure of carazolol, the bound ligand, is shown on the right.

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