7v0s
Local refinement of RhAG/CE trimer, class 1 of erythrocyte ankyrin-1 complexLocal refinement of RhAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex
Structural highlights
Disease[RHCE_HUMAN] Rh deficiency syndrome. The disease is caused by variants affecting the gene represented in this entry. Function[RHCE_HUMAN] May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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