Speaker
Description
Intrinsically disordered proteins (IDPs) lack clearly defined structure and are therefore highly flexible and easily adaptable to different binding partners. This makes them important players in many biological processes, often with vital regulatory functions. Their dynamic features and broad range of interaction modes, however, render them difficult to study and analyzing their complexes often requires integrated approaches. Integrating complementary parameters from of nuclear magnetic resonance (NMR) and single molecule fluorescence approaches allowed us to describe the conformational landscape of IDPs at molecular resolution and promises to shed new light onto various biological processes.
Among those counts clathrin mediated endocytosis. The early phases of clathrin mediated endocytosis are organized through a highly complex interaction network mediated by clathrin associated sorting proteins (CLASPs) that comprise long intrinsically disordered regions (IDRs). We characterize the IDRs of those CLASPs in their entirety and at molecular resolution, uncovering a plethora of interactions of various strengths and dynamic features with their endocytic interaction partners, proposing a rationale for how first interactions and dynamics rearrangement of partners take place during the uptake of a coated vesicle.
| Submitting to: | Integrative Computational Biology workshop |
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