Crystal structure of the heterotrimeric integrin-binding region of laminin-111

Laminins are cell - adhesive glycoproteins that are essential for basement membrane assembly and function. Integrins are important laminin receptors, but their binding site on the heterotrimeric laminin s is poorly defined structurally. We report the crystal structure at 2.13 Å resolution of a minimal integrin - binding fragment of mouse laminin - 111, consisting of ~50 resid ues of α 1 β 1 γ 1 coiled coil and the first three lam inin G - like (LG) domains of the α 1 chain . The LG domains adopt a triangular arrangem ent, with the C - terminus of the coiled coil situated between LG1 and LG2. The critical integrin - binding glutamic acid residue in the γ 1 chain tail is surface - exposed and predicted to bind to the metal ion - dependent adhesion site in the integrin β 1 subunit. Additional contacts to the integrin are likely to be made by the LG1 and LG2 surfaces adjacent to the γ 1 chain tail, which are notably conserved and free of obstructing glycans