Kenneth Jacobson Research Images
In this representation, the newly determined structure of the A2A receptor for adenosine is shown surrounding its synthetic agonist, a molecule that turns on the receptor. The spiral shapes and the slim connecting loops represent the receptor protein, winding back and forth through the cell membrane. The central (red) part of the agonist is critical for activation of the receptor. The top (tan-colored) part of the agonist, facing the outside of the cell, acts like arms to fill much of the remaining space in the binding site and stabilize the receptor, in order to obtain a crystallized structure. Source: Francesca Deflorian, Ph.D., NIDDK, NIH
Molecular model of a homodimeric A2A adenosine receptor containing a bound conjugate of a PAMAM (polyamidoamine) dendrimer and an A2A agonist, CGS21680. In this model, the multivalent dendrimer conjugate is able to bridge both binding sites of the dimeric receptor. The carbon atoms of PAMAM and the covalently attached 31 moieties of CGS21680 are colored in green.
This dendrimer conjugate potently inhibits the aggregation of human platelets induced by ADP.
Page last updated: March 11, 2011