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Abstract:
Clathrin triskelions form the lattice that organizes recruitment of
proteins to coated pits and helps drive Vesiculation of the lipid
bilayer. We report the crystal structure at 2.6 Angstrom resolution of a
55 kDa N-terminal fragment from the 190 kDa clathrin heavy chain. The
structure comprises the globular "terminal domain" and the linker that
joins it to the end of a triskelion leg. The terminal domain is a
seven-blade beta propeller, a structure well adapted to interaction with
multiple partners, such as the AP-1 and AP-2 sorting adaptor complexes
and the nonvisual arrestins. The linker is an alpha-helical zigzag
emanating from the propeller domain. We propose that this simple motif
may extend into the rest of the clathrin leg.
