ArticleThe Journal of biological chemistry2011
Determination of structural models of the complex between the cytoplasmic domain of erythrocyte band 3 and ankyrin-R repeats 13-24.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Transport mechanism of the SLC4 proteins-Lessons from recent structural and computational studies.The Journal of biological chemistry · 2026Review
- Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025Review
- A novel approach to modeling side chain ensembles of the bifunctional spin label RX.bioRxiv : the preprint server for biology · 2023Article
- Comparative evaluation of spin-label modeling methods for protein structural studies.Biophysical journal · 2022Article
- Structure, dynamics and assembly of the ankyrin complex on human red blood cell membrane.Nature structural & molecular biology · 2022Article
- Architecture of the human erythrocyte ankyrin-1 complex.Nature structural & molecular biology · 2022Article
- Protein functional dynamics from the rigorous global analysis of DEER data: Conditions, components, and conformations.The Journal of general physiology · 2021Article
- Methodology for rigorous modeling of protein conformational changes by Rosetta using DEER distance restraints.PLoS computational biology · 2021Article
- Evidence of a structural and functional ammonium transporter RhBG·anion exchanger 1·ankyrin-G complex in kidney epithelial cells.The Journal of biological chemistry · 2015Article
- Single-molecule FRET reveals hidden complexity in a protein energy landscape.Structure (London, England : 1993) · 2015Article
- Automated structure refinement for a protein heterodimer complex using limited EPR spectroscopic data and a rigid-body docking algorithm: a three-dimensional model for an ankyrin-CDB3 complex.The journal of physical chemistry. B · 2014Article
- Spectrin and phospholipids - the current picture of their fascinating interplay.Cellular & molecular biology letters · 2014Review
- mtsslSuite:Molecular physics · 2013Article
- Use of electron paramagnetic resonance to solve biochemical problems.Biochemistry · 2013Review
- Structural arrangement of the intracellular Ca2+ binding domains of the cardiac Na+/Ca2+ exchanger (NCX1.1): effects of Ca2+ binding.The Journal of biological chemistry · 2013Article
- Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane.The Journal of biological chemistry · 2013Article
- Locating a lipid at the portal to the lipoxygenase active site.Biophysical journal · 2012Article
- Identification of contact sites between ankyrin and band 3 in the human erythrocyte membrane.Biochemistry · 2012Article
- Refined views of multi-protein complexes in the erythrocyte membrane.Blood cells, molecules & diseases · 2012Review
- The global analysis of DEER data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
The adaptor protein ankyrin-R interacts via its membrane binding domain with the cytoplasmic domain of the anion exchange protein (AE1) and via its spectrin binding domain with the spectrin-based membrane skeleton in human erythrocytes. This set of interactions provides a bridge between the lipid bilayer and the membrane skeleton, thereby stabilizing the membrane. Crystal structures for the dimeric cytoplasmic domain of AE1 (cdb3) and for a 12-ankyrin repeat segment (repeats 13-24) from the membrane binding domain of ankyrin-R (AnkD34) have been reported. However, structural data on how these proteins assemble to form a stable complex have not been reported. In the current studies, site-directed spin labeling, in combination with electron paramagnetic resonance (EPR) and double electron-electron resonance, has been utilized to map the binding interfaces of the two proteins in the complex and to obtain inter-protein distance constraints. These data have been utilized to construct a family of structural models that are consistent with the full range of experimental data. These models indicate that an extensive area on the peripheral domain of cdb3 binds to ankyrin repeats 18-20 on the top loop surface of AnkD34 primarily through hydrophobic interactions. This is a previously uncharacterized surface for binding of cdb3 to AnkD34. Because a second dimer of cdb3 is known to bind to ankyrin repeats 7-12 of the membrane binding domain of ankyrin-R, the current models have significant implications regarding the structural nature of a tetrameric form of AE1 that is hypothesized to be involved in binding to full-length ankyrin-R in the erythrocyte membrane.
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