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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
30
|
| pubmed:dateCreated |
1998-8-20
|
| pubmed:abstractText |
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:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
18681-4
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9668035-Amino Acid Sequence,
pubmed-meshheading:9668035-Animals,
pubmed-meshheading:9668035-Ankyrin Repeat,
pubmed-meshheading:9668035-Ankyrins,
pubmed-meshheading:9668035-Computer Simulation,
pubmed-meshheading:9668035-Enzyme Stability,
pubmed-meshheading:9668035-Humans,
pubmed-meshheading:9668035-Models, Molecular,
pubmed-meshheading:9668035-Molecular Sequence Data,
pubmed-meshheading:9668035-Protein Conformation,
pubmed-meshheading:9668035-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:9668035-Structure-Activity Relationship
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Structure of the ankyrin-binding domain of alpha-Na,K-ATPase.
|
| pubmed:affiliation |
Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|