In this work is explained how sarcomeric filaments are associated with nonfilamentous proteins which are highly dynamic in terms of their temporal distribution and spatial localization. These components lead to dynamic interactomes and link largely structural filament system to a broad range of signaling molecules (via anchoring). Protein-protein interactions are mediated via intermolecular beta-sheets.
The paper describes conformational changes of tandem CH domains of human alpha-actinin which are needed for its binding to F-actin. This is an important contribution to the understanding of the mechanism of binding of alpha-actinin to actin cytoskeleton since the conformational changes lead to exposure and/or changes in the accessible surface of alpha-actinin which in turn affects the binding other proteins.
In this work we report the preliminary crystallographic analysis of the extracellular portion of human epithelial cell adhesion molecule, EpCAM. This glycoprotein helps to regulate an array of developmental processes including cell migration, cell proliferation and differentiation, and has emerged as a target for anticancer therapies. Structural studies of this molecule are of great interest to the wider academic community. We determined the spacegroup, unit cell dimensions, and contents of the asymmetric unit, are an excellent introduction for solving the 3D structure of the protein.