The conference «Inter-domain communication among the domains mediated by intrinsically disordered region (IDR) – the role of intramolecular ‘fly-casting’» by Prof. Shin-ichi Tate from Hiroshima University (Japan) will be held  at the Institute of Analytical Sciences (Amphitheater CRMN) the 13th december 2016, 10 am.



Abstract :

Since the finding that many parts of proteins in cells are unfolded under physiological condition, studies have been conducted to explore the functional roles of the unstructured elements of proteins; which are called as intrinsically disordered regions, IDRs. In a past decade of IDR research, a variety of novel functions specifically associated with the IDRs have been collected. The made the IDRs recognized as the distinct elements enabling the novel roles that have never been achieved by folded proteins.
One of the most characteristic functions of IDRs is realized in the process of the ligand binding. The unstructured element has a greater radius of gyration over the folded protein having the same number of residues. The larger molecular radius of the IDR allows the wider space of search for the target and facilitates k on process and eventually increases the affinity. In other words, IDR captures the target at more distant position over the anticipated contact of the folded protein, and reels it up by folding in the binding, which is ‘fly-casting’ mechanism.
Some proteins have the architecture comprising of the folded domains linked by flexible linkers or IDRs. In the molecular evolution, such multi-domain architectures should have gained functional advantages, however, they remain elusive in most of the cases. In this presentation, I will figure out how the folded domains linked by IDR interplay to exert the function, in which the engagement of the intra-molecular ‘fly-casting’ mechanism is emphasized.
Our results will add a new role of IDR and make it convinced that the IDRs connecting folded domains are not mere tethering ropes but they have specific functions that are readily altered by the mutations within, as common in the folded protein parts. IDRs are also the parts generated through the evolutional challenges.


Prof. Shin-ichi Tate from the department of Mathematical and Life Sciences, School of Science, Hiroshima University, Japan and the Research Center for the Mathematics on Chromatin Live Dynamics (RcMcD), Hiroshima University, Japan