%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%% ULB Machine Learning Group (MLG) S E M I N A R %%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%% Apologies for cross-postings. Please send it to interested colleagues and students. Thanks! Title: "Structure, Unstructure and Alternative Splicing" by: Dr. Philip Kim, The Donnelly Centre for Cellular and Biomolecular Research Banting and Best Department of Medical Research Departments of Molecular Genetics and Computer Science University of Toronto http://www.kimlab.org http://www.thedonnellycentre.utoronto.ca When: 22 February 2012 at 16:00 (until 17:30) Where: Building NO, Sale Solvay (5th floor in the rotule) Université Libre de Bruxelles Boulevard du Triomphe 1050 Bruxelles Campus access : http://mlg.ulb.ac.be/access Abstract: Many protein interactions, in particular those in signaling networks, are mediated by peptide recognition domains. These recognize short, linear amino acid stretches on the surface of their cognate partners with high specificity. Residues in these stretches are usually assumed to contribute independently to binding, which has led to a simplified understanding of protein interactions. Conversely, in large binding peptide data sets different residue positions display highly significant correlations for many domains in three distinct families (PDZ, SH3 and WW). These correlation patterns reveal a widespread occurrence of multiple binding specificities and give novel structural insights into protein interactions. For example, a new binding mode of PDZ domains can be predicted and structurally rationalized for DLG1 PDZ1. While protein structure is very important for peptide binding domains, the regions they bind are usually unstructured (intrinsically disordered). These regions are widespread, especially in proteomes of higher eukaryotes, and have been associated with a plethora of different cellular functions. Aside from general importance for signaling networks, they are also important for such diverse processes as protein folding or DNA binding. Leveraging knowledge from systems biology can help to structure the phenomenon. Strikingly, disorder can be partitioned into three biologically distinct phenomena: regions where disorder is conserved but with quickly evolving amino acid sequences (flexible disorder), regions of conserved disorder with also highly conserved amino acid sequence (constrained disorder) and, lastly, non-conserved disorder. I will also introduce new efforts to map protein interactions affected by alternative splicing. Speaker:Dr. Philip Kim is Associate professor at University of Toronto (The Donnelly Centre for Cellular and Biomolecular Research) where he has set up a research group investigating protein interaction and genetic variation His group has pioneered some integrative approaches combining structural and systems knowledge (see Kim et al. Science 2006), as well as methodologies from genetics and network biology (see Kim et al. PNAS 2007), in an active attempt to bring genetic and protein biophysical research closer together. He has also played an import role in the understanding of specificities of the modular domains typically found in proteins. %%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%% MLG http://mlg.ulb.ac.be/ %%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%%