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Updated: Jun 10, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
Asymmetry as the key to clathrin cage assembly
Wouter K den Otter1, Marten R Renes, W J Briels
1Computational BioPhysics, University of Twente, Enschede, The Netherlands. w.k.denotter@utwente.nl
Abstract:
The self-assembly of clathrin proteins into polyhedral cages is simulated for the first time (to our knowledge) by introducing a coarse-grain triskelion particle modeled after clathrin's characteristic shape. The simulations indicate that neither this shape, nor the antiparallel binding of four legs along the lattice edges, is sufficient to induce cage formation from a random solution. Asymmetric intersegmental interactions, which probably result from a patchy distribution of interactions along the legs' surfaces, prove to be crucial for the efficient self-assembly of cages.
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