The determined crystal structure of extracellular part of EpCAM dimer was presented along with the models of transmembrane helix dimer and tetrameric adhesion unit. Additionally, the proposed model of adhesion network formed by cis-interactions of adjacent adhesion units was presented to highlight the adhesion function of EpCAM, one of the rare adhesion molecules with determined threedimensional structure.
B.03 Paper at an international scientific conferenceCOBISS.SI-ID: 35457797
We are one of the rare research groups that perform research with EpCAM at the molecular level. We can work with entire EpCAM molecule as well as with the individual domains. Presentation of our research at the prestigious University of Groningen has been the basis for establishing cooperation with a group of prof. Giepmans.
B.04 Guest lectureCOBISS.SI-ID: 30531589
University of Zurich, Institute for Biochemistry, Zurich On the basis of our lecture where we presented different roles of thyroglobulin type 1 domains in proteins that are structurally and functionally unrelated we established a collaboration with an exceptional research group of prof. A. Plueckthun from the University of Zurich. The fact that we solved the crystal structure of EpCAM enabled us the access to the library of DARPins (Designed Ankyrin Repeat Proteins), proteins that can specifically bind to EpCAM. DARPins are new generation of protein therapeutics that represents an excellent substitute for monoclonal antibodies.
B.04 Guest lectureCOBISS.SI-ID: 34956293
In the lecture we presented first joint results of collaboration with the group of Prof. Plückthun. 3D models of complexes of EpCAM and DARPins supported with experimental results were discussed.
B.04 Guest lectureCOBISS.SI-ID: 36596485