Similarly to the soluble integrins, recombinantly expressed domains of collagens and of laminin-332 provide insights in the integrin-mediated cell-matrix interactions. In contrast to the RGD-peptide motif, the integrin recognition sites in collagens and laminins depend on the quaternary structure and three-dimensional conformation, i.e. triple helix of collagens and the coiled-coil-stabilized G-domain of laminin-332 (Eble, 2001; Eble et al, 1993; Golbik et al, 2000; Kern et al, 1993; Kühn & Eble, 1994; Künneken et al, 2004; Navdaev et al, 2008; Saccà et al, 2002). Moreover, the mini-integrin-ligands are suitable antigens to produce functional antibodies for the analysis of integrin-ligand interactions.
The mini-collagen containing the a2b1integrin binding site has been used to measure mechanical forces between individual integrins and their ligands (Ligezowska A, et al. 2011, Boye, 2013 #1; Niland S, et al. 2011).