Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker

Cell. 1998 Nov 13;95(4):563-73. doi: 10.1016/s0092-8674(00)81623-2.


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 A 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arrestins / metabolism
  • Clathrin / chemistry*
  • Clathrin / metabolism
  • Crystallography, X-Ray
  • Helix-Loop-Helix Motifs
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Protein Structure, Tertiary
  • Rats
  • beta-Arrestins


  • Arrestins
  • Clathrin
  • Peptide Fragments
  • beta-Arrestins

Associated data

  • PDB/1BPO