  We analyze the stability of micro-domains of ligand-receptor bonds that
mediate the adhesion of biological model membranes. After evaluating the
effects of membrane fluctuations on the binding affinity of a single bond, we
characterize the organization of bonds within the domains by theoretical means.
In a large range of parameters, we find the commonly suggested dense packing to
be separated by a free energy barrier from a regime in which bonds are sparsely
distributed. If bonds are mobile, a coexistence of the two regimes should
emerge, which agrees with recent experimental observations.
