3UD1
Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin
Summary for 3UD1
| Entry DOI | 10.2210/pdb3ud1/pdb |
| Related | 3UD2 |
| Descriptor | Ankyrin-1, ETHANOL (3 entities in total) |
| Functional Keywords | beta sandwich, zu5, adapter protein, spectrin binding, cytoskeleton, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform Er1: Cytoplasm, cytoskeleton. Isoform Mu17: Membrane. Isoform Mu18: Sarcoplasmic reticulum (Probable). Isoform Mu19: Sarcoplasmic reticulum (Probable). Isoform Mu20: Sarcoplasmic reticulum (Probable): P16157 |
| Total number of polymer chains | 3 |
| Total formula weight | 108808.68 |
| Authors | Yasunaga, M.,Ipsaro, J.J.,Mondragon, A. (deposition date: 2011-10-27, release date: 2012-02-22, Last modification date: 2023-09-13) |
| Primary citation | Yasunaga, M.,Ipsaro, J.J.,Mondragon, A. Structurally Similar but Functionally Diverse ZU5 Domains in Human Erythrocyte Ankyrin. J.Mol.Biol., 417:336-350, 2012 Cited by PubMed Abstract: The metazoan cell membrane is highly organized. Maintaining such organization and preserving membrane integrity under different conditions are accomplished through intracellular tethering to an extensive, flexible protein network. Spectrin, the principal component of this network, is attached to the membrane through the adaptor protein ankyrin, which directly bridges the interaction between β-spectrin and membrane proteins. Ankyrins have a modular structure that includes two tandem ZU5 domains. The first domain, ZU5A, is directly responsible for binding β-spectrin. Here, we present a structure of the tandem ZU5 repeats of human erythrocyte ankyrin. Structural and biophysical experiments show that the second ZU5 domain, ZU5B, does not participate in spectrin binding. ZU5B is structurally similar to the ZU5 domain found in the netrin receptor UNC5b supramodule, suggesting that it could interact with other domains in ankyrin. Comparison of several ZU5 domains demonstrates that the ZU5 domain represents a compact and versatile protein interaction module. PubMed: 22310050DOI: 10.1016/j.jmb.2012.01.041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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