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http://purl.uniprot.org/citations/35835865http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35835865http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35835865http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.org/dc/terms/identifier"doi:10.1038/s41594-022-00792-w"xsd:string
http://purl.uniprot.org/citations/35835865http://purl.org/dc/terms/identifier"doi:10.1038/s41594-022-00792-w"xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Kim K."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Kim K."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Noble A.J."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Noble A.J."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Clarke O.B."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Clarke O.B."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Cali T."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Cali T."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Johnston J.D."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Johnston J.D."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Vallese F."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Vallese F."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Yen L.Y."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/author"Yen L.Y."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/pages"706-718"xsd:string
http://purl.uniprot.org/citations/35835865http://purl.uniprot.org/core/pages"706-718"xsd:string