Structural highlights
7v0k is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | Electron Microscopy, Resolution 2.4Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
RHCE_HUMAN Rh deficiency syndrome. The disease is caused by variants affecting the gene represented in this entry.
Function
RHCE_HUMAN Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Mediates the primary membrane attachment site for ANK1 when associated with RHAG (PubMed:35835865). May participate in the ammonium and carbon dioxide transport through the heterotrimer form (Probable).[1]
Publication Abstract from PubMed
The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.
Architecture of the human erythrocyte ankyrin-1 complex.,Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w. , Epub 2022 Jul 14. PMID:35835865[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB. Architecture of the human erythrocyte ankyrin-1 complex. Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w., Epub 2022 Jul 14. PMID:35835865 doi:http://dx.doi.org/10.1038/s41594-022-00792-w
- ↑ Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Cali T, Clarke OB. Architecture of the human erythrocyte ankyrin-1 complex. Nat Struct Mol Biol. 2022 Jul;29(7):706-718. doi: 10.1038/s41594-022-00792-w., Epub 2022 Jul 14. PMID:35835865 doi:http://dx.doi.org/10.1038/s41594-022-00792-w
