Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain.
Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain.
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DOI:
10.1016/j.chom.2010.03.005
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发表时间:
2010-04-22
影响因子:
30.3
通讯作者:
Weissenhorn W
中科院分区:
文献类型:
--
作者:
Hinz A;Miguet N;Natrajan G;Usami Y;Yamanaka H;Renesto P;Hartlieb B;McCarthy AA;Simorre JP;Göttlinger H;Weissenhorn W
The restriction factor Bst2/tetherin contains two membrane anchors which are employed to retain some enveloped viruses including HIV-1 tethered to the plasma membrane in the absence of virus encoded antagonists. The 2.77 Å crystal structure of the extracellular core presented here reveals a parallel 90 Å long disulfide linked coiled-coil domain while the complete extracellular domain forms an extended 170 Å long rod-like structure based on small angle X-ray scattering data. Mutagenesis analyses indicate that both the coiled-coil and the N-terminal region are required for retention of HIV-1, suggesting that the elongated structure can function as a molecular ruler to bridge long distances. The structure reveals substantial irregularities and instabilities throughout the coiled-coil, which contribute to its low stability in the absence of disulfide bonds. We propose that the irregular coiled-coil provides conformational flexibility and ensures that Bst2/tetherin anchoring in the plasma and the newly formed virus membrane do not interfere with budding.
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DOI:
10.1107/s0907444905036693
发表时间:
2006-01-01
影响因子:
2.2
作者:
Evans, P
通讯作者:
Evans, P
DOI:
10.1073/pnas.0606741103
发表时间:
2006-11-21
影响因子:
11.1
作者:
Blankenfeldt, Wulf;Thoma, Nicolas H.;Schlichting, Ilme
通讯作者:
Schlichting, Ilme
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
5.6
作者:
Burkhard, P;Ivaninskii, S;Lustig, A
通讯作者:
Lustig, A
影响因子:
30.3
作者:
Goffinet, Christine;Allespach, Ina;Keppler, Oliver T.
通讯作者:
Keppler, Oliver T.