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  • Title: Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals.
    Author: Yamaguchi T, Fujii T, Abe Y, Hirai T, Kang D, Namba K, Hamasaki N, Mitsuoka K.
    Journal: J Struct Biol; 2010 Mar; 169(3):406-12. PubMed ID: 20005958.
    Abstract:
    The C-terminal membrane domain of erythrocyte band 3 functions as an anion exchanger. Here, we report the three-dimensional (3D) structure of the membrane domain in an inhibitor-stabilized, outward-open conformation at 18A resolution. Unstained, frozen-hydrated tubular crystals containing the membrane domain of band 3 purified from human red blood cells (hB3MD) were examined using cryo-electron microscopy and iterative helical real-space reconstruction (IHRSR). The 3D image reconstruction of the tubular crystals showed the molecular packing of hB3MD dimers with dimensions of 60 x 110 A in the membrane plane and a thickness of 70A across the membrane. Immunoelectron microscopy and carboxyl-terminal digestion demonstrated that the intracellular surface of hB3MD was exposed on the outer surface of the tubular crystal. A 3D density map revealed that hB3MD consists of at least two subdomains and that the outward-open form is characterized by a large hollow area on the extracellular surface and continuous density on the intracellular surface.
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