Crystal structure of a 12 ANK repeat stack from human ankyrinR

Peter Michaely, Diana R. Tomchick, Mischa Machius, Richard G W Anderson

Research output: Contribution to journalArticlepeer-review

171 Scopus citations


Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrinactin cytoskeleton. The N-terminal, 'membrane-binding' domain of ankyrins contains 24 ANK repeats and mediates most binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO3 anion exchanger, voltagegated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. Here we report the crystal structure of a human ankyrinR construct containing ANK repeats 13-24 and a portion of the spectrin-binding domain. The ANK repeats are observed to form a contiguous spiral stack with which the spectrin-binding domain fragment associates as an extended strand. The structural information has been used to construct models of all 24 repeats of the membrane-binding domain as well as the interactions of the repeats with the Cl/HCO3 anion exchanger and clathrin. These models, together with available binding studies, suggest that ion transporters such as the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.

Original languageEnglish (US)
Pages (from-to)6387-6396
Number of pages10
JournalEMBO Journal
Issue number23
StatePublished - Dec 2 2002


  • ANK
  • Anion exchanger
  • Ankyrin
  • Clathrin
  • Spectrin

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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