Membrane cholesterol modulates the dimer interface of the -adrenergic receptor. Coarse-grain molecular dynamics simulations show that the receptor dimerization is modulated by membrane cholesterol content. With increasing membrane cholesterol, the transmembrane helices of the -adrenergic receptor that comprise the dimer interface, display variation. At low membrane cholesterol, the dimer interface is mainly composed of transmembrane helices IV and V. Interestingly, at high membrane cholesterol, the dimer interface consists of transmembrane helices I and II. These results imply that dimer plasticity, induced by varying membrane cholesterol content, is potentially useful in drug development. Data obtained from [40]. See text for more details.