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Asymmetry as the key to clathrin cage assembly.

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.

SUBMITTER: den Otter WK

PROVIDER: S-EPMC2920741 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Asymmetry as the key to clathrin cage assembly.

den Otter Wouter K WK Renes Marten R MR Briels W J WJ

Biophysical journal 20100801 4

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 ...[more]

PMID: 20713007

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