Asymmetry as the key to clathrin cage assembly.
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.
den Otter
Wouter K
WK
Computational BioPhysics, University of Twente, Enschede, The Netherlands. w.k.denotter@utwente.nl
Renes
Marten R
MR
Briels
W J
WJ
D002966:Clathrin / Q000737:chemistry*; D003198:Computer Simulation; D008958:Models, Molecular; D009010:Monte Carlo Method; D013816:Thermodynamics
D002966:Clathrin