The Stetefeld lab has a long-standing interest in exploiting the structure-property relationship of key components in extracellular higher-order signaling complexes. Starting with the very first high-resolution X-ray crystal structure of such a signaling component, the study of the basement membrane protein laminin  helped to establish the field of structural biology of higher order matrix assemblies, and it has since become a standard reference in the field.
The lab expanded studies from individual domains over tandem arrangements towards signaling assemblies. For example, the unravelling of agrin-mediated neuromuscular junction formation [2,3] and the exploring of the effect of alternative mRNA splice inserts in muscular dystrophy [4,5] contributed significantly to a molecular understanding of underlying diseases. Other avenues of research included collagen assemblies via phage-based foldon systems [6,7], Cadherin super-assemblies  and integrin-snake venom lectin interactions .
Most recently, we have published work about Netrin-1 and its interaction with the dependence receptor UNC5 and Netrin-4 disrupting basement membrane networks [10,11]. Studies of these protein-protein networks are extremely important for the development of new therapeutic approaches in numerous cancers and neurodegenerative diseases. By applying AI-technology to this mostly transient protein-protein interaction networks it is envisioned to design and characterize specific mediators that allow for targeted apoptosis of specific cancer cells.
 Stetefeld et al. JMB, 1996  Stetefeld et al. Nature Structural Biology, 2001  Mascarenhas et al. EMBO J, 2003  Stetefeld et al. Structure, 2004  Stetefeld & Ruegg TIBS, 2005  Stetefeld et al. Structure, 2004  Boudko et al. JMB, 2004  Haeussinger et al. EMBO J, 2004  Eble et al. PlosBiol, 2017  Grandin et al. Cancer Cell, 2016  Reuten et al. Nature Communications, 2017