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| Subject Categories: Structural Biology | Cell & Tissue Architecture |
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| The EMBO Journal
(2002) 21, 6387–6396, doi: 10.1093/emboj/cdf651 |
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| Crystal structure of a 12 ANK repeat stack from human ankyrinR |
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| Peter Michaely1, Diana R. Tomchick2, Mischa Machius2 and Richard G.W. Anderson1 |
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1 Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75235-9039, USA 2 Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235-9039, USA To whom correspondence should be addressed Peter Michaely, peter.michaely@utsouthwestern.edu Received 25 July 2002; Revised 14 October 2002; Accepted 17 October 2002. |
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| Abstract |
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| Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin−actin 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, voltage-gated 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. |
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| Keywords: anion exchanger, ANK, ankyrin, clathrin, spectrin |
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