Crystal Structure of the N-Terminal Domain of Nup358/RanBP2

Key steps in mRNA export are the nuclear assembly of messenger ribonucleoprotein particles (mRNPs), the translocation of mRNPs through the nuclear pore complex (NPC), and the mRNP remodeling events at the cytoplasmic side of the NPC. Nup358/RanBP2 is a constituent of the cytoplasmic filaments of the NPC specific to higher eukaryotes and provides a multitude of binding sites for the nucleocytoplasmic transport machinery. Here, we present the crystal structure of the Nup358 N-terminal domain (NTD) at 0.95 Å resolution. The structure reveals an α-helical domain that harbors three central tetratricopeptide repeats (TPRs), flanked on each side by an additional solvating amphipathic α helix. Overall, the NTD adopts an unusual extended conformation that lacks the characteristic peptide-binding groove observed in canonical TPR domains. Strikingly, the vast majority of the NTD surface exhibits an evolutionarily conserved, positive electrostatic potential, and we demonstrate that the NTD possesses the capability to bind single-stranded RNA in solution. Together, these data suggest that the NTD contributes to mRNP remodeling events at the cytoplasmic face of the NPC

Qualitative Modelling in Embodiment Design - Investigating the Contact and Channel Approach Through Analysis of Projects

Purposeful qualitative modelling of embodiment function relations is a challenge in embodiment design. This contribution investigates the applicability and usefulness of the Contact and Channel Approach as a qualitative modelling approach in a survey study. From 23 development and research projects, advantages and challenges regarding applicability and usefulness are identified. A further result is that many different models are used additionally to the Contact and Channel Approach. Based on the findings, research potential for optimization and development of links to other models emerges