Intermolecular contacts between integrin LFA-1 (?(L)?(2)) and ICAM-1 derive solely from the integrin ?(L) I domain and the first domain (D1) of ICAM-1. This study presents a crystal structure of the engineered complex of the ?(L) I domain and ICAM-1 D1. Previously, we engineered the I domain for high affinity by point mutations that were identified by a directed evolution approach. In order to examine ?(L) I domain allostery between the C-terminal ?7-helix (allosteric site) and the metal-ion dependent adhesion site (active site), we have chosen a high affinity variant without mutations directly influencing either the position of the ?7-helix or the active sites. In our crystal, the ?(L) I domain was found to have a high affinity conformation to D1 with its ?7-helix displaced downward away from the binding interface, recapitulating a current understanding of the allostery in the I domain and its linkage to neighboring domains of integrins in signaling. To enable soluble D1 of ICAM-1 to fold on its own, we also engineered D1 to be functional by mutations, which were found to be those that would convert hydrogen bond networks in the solvent-excluded core into vdW contacts. The backbone structure of the ?-sandwich fold and the epitope for I domain binding of the engineered D1 were essentially identical to those of wild-type D1. Most deviations in engineered D1 were found in the loops at the N-terminal region that interacts with human rhinovirus (HRV). Structural deviation found in engineered D1 was overall in agreement with the function of engineered D1 observed previously, i.e., full capacity binding to ?(L) I domain but reduced interaction with HRV.