1BG5

CRYSTAL STRUCTURE OF THE ANKYRIN BINDING DOMAIN OF ALPHA-NA,K-ATPASE AS A FUSION PROTEIN WITH GLUTATHIONE S-TRANSFERASE

Summary for 1BG5

• Entry DOI: 10.2210/pdb1bg5/pdb
• Descriptor: FUSION PROTEIN OF ALPHA-NA,K-ATPASE WITH GLUTATHIONE S-TRANSFERASE (2 entities in total)
• Functional Keywords: ankyrin binding, atpase, glutathione-s-transferase, carrier crystallization, ion transport
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 29528.21

Authors

Zhang, Z.,Devarajan, P.,Morrow, J.S. (deposition date: 1998-06-05, release date: 1999-01-13, Last modification date: 2024-05-22)

Primary citation

Zhang, Z.,Devarajan, P.,Dorfman, A.L.,Morrow, J.S.
Structure of the ankyrin-binding domain of alpha-Na,K-ATPase.
J.Biol.Chem., 273:18681-18684, 1998

PubMed Abstract: The 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.

PubMed: 9668035
DOI: 10.1074/jbc.273.30.18681

Experimental method

X-RAY DIFFRACTION (2.6 Å)