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To advance understanding of BST2 function, we have determined a 2.6\u00a0\u212b crystal structure of the extracellular domain of the bacterially expressed recombinant human protein, residues 47\u2013152, under reducing conditions. The structure forms a single long helix that associates as a parallel dimeric coiled coil over its C-terminal two-thirds, while the N-terminal third forms an antiparallel four-helix bundle with another dimer, creating a global tetramer. We also report the 3.45\u00a0\u212b resolution structure of BST2(51-151) prepared by expression as a secreted protein in HEK293T cells. This oxidized construct forms a dimer in the crystal that is superimposable with the reduced protein over the C-terminal two-thirds of the molecule, and its N terminus suggests pronounced flexibility. Hydrodynamic data demonstrated that BST2 formed a stable tetramer under reducing conditions and a dimer when oxidized to form disulfide bonds. A mutation that selectively disrupted the tetramer (L70D) increased protein expression modestly but only reduced antiviral activity by approximately threefold. Our data raise the possibility that BST2 may function as a tetramer at some stage, such as during trafficking, and strongly support a model in which the primary functional state of BST2 is a parallel disulfide-bound coiled coil that displays flexibility toward its N terminus.<\/jats:p>","DOI":"10.1073\/pnas.1008206107","type":"journal-article","created":{"date-parts":[[2010,9,30]],"date-time":"2010-09-30T03:59:58Z","timestamp":1285819198000},"page":"17951-17956","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":87,"title":["Structural and functional studies on the extracellular domain of BST2\/tetherin in reduced and oxidized conformations"],"prefix":"10.1073","volume":"107","author":[{"given":"Heidi L.","family":"Schubert","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650; and"}]},{"given":"Qianting","family":"Zhai","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650; and"}]},{"given":"Virginie","family":"Sandrin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650; and"}]},{"given":"Debra M.","family":"Eckert","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650; and"}]},{"given":"Mitla","family":"Garcia-Maya","sequence":"additional","affiliation":[{"name":"Randall Division of Cell and Molecular Biophysics, King\u2019s College London, New Hunt\u2019s House, Guy\u2019s Campus, London, SE1 1UL, United Kingdom"}]},{"given":"Louise","family":"Saul","sequence":"additional","affiliation":[{"name":"Randall Division of Cell and Molecular Biophysics, King\u2019s College London, New Hunt\u2019s House, Guy\u2019s Campus, London, SE1 1UL, United Kingdom"}]},{"given":"Wesley I.","family":"Sundquist","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650; and"}]},{"given":"Roberto A.","family":"Steiner","sequence":"additional","affiliation":[{"name":"Randall Division of Cell and Molecular Biophysics, King\u2019s College London, New Hunt\u2019s House, Guy\u2019s Campus, London, SE1 1UL, United Kingdom"}]},{"given":"Christopher P.","family":"Hill","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650; and"}]}],"member":"341","published-online":{"date-parts":[[2010,9,29]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1038\/nri2314","article-title":"Interferon-inducible antiviral effectors","volume":"8","author":"Sadler AJ","year":"2008","unstructured":"AJ Sadler, BR Williams, Interferon-inducible antiviral effectors. 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