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CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASECRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe ankyrin 33-residue repeating motif, an L-shaped structure with protruding beta-hairpin tips, mediates specific macromolecular interactions with cytoskeletal, membrane, and regulatory proteins. The association between ankyrin and alpha-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. alpha-Na,K-ATPase binds both red cell ankyrin (AnkR, a product of the ANK1 gene) and Madin-Darby canine kidney cell ankyrin (AnkG, 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 (Kd = 118 +/- 50 nM). The three-dimensional structure (2.6 A) of this minimal ankyrin-binding motif, crystallized as the fusion protein, reveals a 7-residue loop with one charged hydrophilic face capping a double beta-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 beta-hairpin tips of multiple ankyrin repeat units. Structure of the ankyrin-binding domain of alpha-Na,K-ATPase.,Zhang Z, Devarajan P, Dorfman AL, Morrow JS J Biol Chem. 1998 Jul 24;273(30):18681-4. PMID:9668035[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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