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Journal Article

Two-dimensional structure of the membrane domain of human Band 3, the anion transport protein of the erythrocyte membrane

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Citation

Wang, D. N., Kühlbrandt, W., Sarabia, V. E., & Reithmeier, R. A. (1993). Two-dimensional structure of the membrane domain of human Band 3, the anion transport protein of the erythrocyte membrane. EMBO Journal, 12(6), 2233-2239. doi:10.1002/j.1460-2075.1993.tb05876.x.


Cite as: http://hdl.handle.net/21.11116/0000-0007-DD92-B
Abstract
The membrane domain of human erythrocyte Band 3 protein (Mr 52,000) was reconstituted with lipids into two-dimensional crystals in the form of sheets or tubes. Crystalline sheets were monolayers with six-fold symmetry (layer group p6, a = b = 170 A, gamma = 60 degrees), whereas the symmetry of the tubular crystals was p2 (a = 104 A, b = 63 A, gamma = 104 degrees). Electron image analysis of negatively stained specimens yielded projection maps of the protein at 20 A resolution. Maps derived from both crystal forms show that the membrane domain is a dimer of two monomers related by two-fold symmetry, with each monomer consisting of three subdomains. In the dimer, two subdomains of each monomer form a roughly rectangular core (40 x 50 A in projection), surrounding a central depression. The third subdomain of the monomer measures approximately 15 x 25 A in projection and appears to be connected to the other two by a flexible link. We propose that the central depression may represent the channel for anion transport while the third subdomain appears not to be directly involved in channel formation.