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J Biol Chem, Vol. 273, Issue 30, 18681-18684, July 24, 1998

COMMUNICATION
Structure of the Ankyrin-binding Domain of -Na,K-ATPase

Zhushan Zhang, Prasad Devarajan^¶, Adam L. Dorfman, and Jon S. Morrow

From the Departments of  Pathology and ^¶ Pediatrics, Yale University School of Medicine, New Haven, Connecticut 06510

The ankyrin 33-residue repeating motif, an L-shaped structure with protruding -hairpin tips, mediates specific macromolecular interactions with cytoskeletal, membrane, and regulatory proteins. The association between ankyrin and -Na,K-ATPase, a ubiquitous membrane protein critical to vectorial transport of ions and nutrients, is required to assemble and stabilize Na,K-ATPase at the plasma membrane. -Na,K-ATPase binds both red cell ankyrin (Ank_R, a product of the ANK1 gene) and Madin-Darby canine kidney cell ankyrin (Ank_G, a product of the ANK3 gene) utilizing residues 142-166 (SYYQEAKSSKIMESFK NMVPQQALV) in its second cytoplasmic domain. Fusion peptides of glutathione S-transferase incorporating these 25 amino acids bind specifically to purified ankyrin (K_d = 118 ± 50 nM). The three-dimensional structure (2.6 Å) of this minimal ankyrin-binding motif, crystallized as the fusion protein, reveals a 7-residue loop with one charged hydrophilic face capping a double -strand. Comparison with ankyrin-binding sequences in p53, CD44, neurofascin/L1, and the inositol 1,4,5-trisphosphate receptor suggests that the valency and specificity of ankyrin binding is achieved by the interaction of 5-7-residue surface loops with the -hairpin tips of multiple ankyrin repeat units.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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