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7V0K

Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map)

This is a non-PDB format compatible entry.
Summary for 7V0K
Entry DOI10.2210/pdb7v0k/pdb
EMDB information26874 26886 26916 26917 26918 26919 26940 26943 26944 26948 26949 26950 26951 26952 26953 26954 26955 26956 26958 26960 26965 26972 26973 26974 26975 26978 26979 26982 26988
DescriptorBlood group Rh(CE) polypeptide, DIUNDECYL PHOSPHATIDYL CHOLINE, [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate, ... (12 entities in total)
Functional Keywordsmembrane protein, anion exchange, erythrocyte, glycoprotein, transport protein-structural protein complex, transport protein/structural protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains10
Total formula weight763985.92
Authors
Vallese, F.,Kim, K.,Yen, L.Y.,Johnston, J.D.,Noble, A.J.,Cali, T.,Clarke, O.B. (deposition date: 2022-05-10, release date: 2022-07-20, Last modification date: 2024-10-16)
Primary citationVallese, F.,Kim, K.,Yen, L.Y.,Johnston, J.D.,Noble, A.J.,Cali, T.,Clarke, O.B.
Architecture of the human erythrocyte ankyrin-1 complex.
Nat.Struct.Mol.Biol., 29:706-718, 2022
Cited by
PubMed Abstract: 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.
PubMed: 35835865
DOI: 10.1038/s41594-022-00792-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.4 Å)
Structure validation

227111

數據於2024-11-06公開中

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