In contrast, the binding thermodynamics of DC-SIGNR were found to differ significantly from those of DC-SIGN. The highly favourable ΔH 0 values obtained in DC-SIGN were significantly reduced for DC-SIGNR binding with all three Gx-DiMans. The ΔH 0 s of DC-SIGNR binding with all three Gx-DiMans were similar, and at ∼half those obtained with DC-SIGN. This result may indicate that only the binding/or unbinding of two CRDs in DC-SIGNR-Gx-DiMan interactions were captured under our experimental conditions. This result is consistent with the Dh studies where DC-SIGNR cross-links with different Gx-DiMans, presumably first using 2 CRDs to form partially bound Gx-DiMan-DC-SIGNR structural units, which then crosslink each other to form large assemblies. The later step may happen over a relatively long period and hence may not be captured in the current measurement.