Cell
Volume 95, Issue 4, 13 November 1998, Pages 563-573
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Article
Atomic Structure of Clathrin: A β Propeller Terminal Domain Joins an α Zigzag Linker

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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 Å 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 β 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 α-helical zigzag emanating from the propeller domain. We propose that this simple motif may extend into the rest of the clathrin leg.

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