7TW2
Cryo-EM structure of human band 3 dimer from red blood cell
This is a non-PDB format compatible entry.
Summary for 7TW2
Entry DOI | 10.2210/pdb7tw2/pdb |
Related | 7TVZ |
EMDB information | 26142 26143 26144 26148 |
Descriptor | Band 3 anion transport protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
Functional Keywords | red blood cell, ankyrin complex, membrane protein, band 3 |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 2 |
Total formula weight | 204210.13 |
Authors | Xia, X.,Liu, S.H.,Zhou, Z.H. (deposition date: 2022-02-06, release date: 2022-06-08, Last modification date: 2024-11-20) |
Primary citation | Xia, X.,Liu, S.,Zhou, Z.H. Structure, dynamics and assembly of the ankyrin complex on human red blood cell membrane. Nat.Struct.Mol.Biol., 29:698-705, 2022 Cited by PubMed Abstract: The cytoskeleton of a red blood cell (RBC) is anchored to the cell membrane by the ankyrin complex. This complex is assembled during RBC genesis and comprises primarily band 3, protein 4.2 and ankyrin, whose mutations contribute to numerous human inherited diseases. High-resolution structures of the ankyrin complex have been long sought-after to understand its assembly and disease-causing mutations. Here, we analyzed native complexes on the human RBC membrane by stepwise fractionation. Cryo-electron microscopy structures of nine band-3-associated complexes reveal that protein 4.2 stabilizes the cytoplasmic domain of band 3 dimer. In turn, the superhelix-shaped ankyrin binds to this protein 4.2 via ankyrin repeats (ARs) 6-13 and to another band 3 dimer via ARs 17-20, bridging two band 3 dimers in the ankyrin complex. Integration of these structures with both prior data and our biochemical data supports a model of ankyrin complex assembly during erythropoiesis and identifies interactions essential for the mechanical stability of RBC. PubMed: 35655099DOI: 10.1038/s41594-022-00779-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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