2X7A

Structural basis of HIV-1 tethering to membranes by the Bst2-tetherin ectodomain

2X7A の概要

• エントリーDOI: 10.2210/pdb2x7a/pdb
• 分子名称: BONE MARROW STROMAL ANTIGEN 2, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: tetherin, gpi-anchor, antiviral defense, b-cell activation, immune system, signal-anchor
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Golgi apparatus, trans-Golgi network: Q10589
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 76364.50

構造登録者

Natrajan, G.,McCarthy, A.A.,Weissenhorn, W. (登録日: 2010-02-25, 公開日: 2010-04-28, 最終更新日: 2024-10-23)

主引用文献

Hinz, A.,Miguet, N.,Natrajan, G.,Usami, Y.,Yamanaka, H.,Renesto, P.,Hartlieb, B.,Mccarthy, A.A.,Simorre, J.P.,Gottlinger, H.,Weissenhorn, W.
Structural Basis of HIV-1 Tethering to Membranes by the Bst-2/Tetherin Ectodomain.
Cell Host Microbe, 7:314-, 2010

PubMed Abstract: The restriction factor BST-2/tetherin contains two membrane anchors employed to retain some enveloped viruses, including HIV-1 tethered to the plasma membrane in the absence of virus-encoded antagonists. The 2.77 A crystal structure of the BST-2/tetherin extracellular core presented here reveals a parallel 90 A long disulfide-linked coiled-coil domain, while the complete extracellular domain forms an extended 170 A 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, ensuring that BST-2/tetherin anchoring both in the plasma membrane and in the newly formed virus membrane is maintained during virus budding.

PubMed: 20399176
DOI: 10.1016/J.CHOM.2010.03.005

実験手法

X-RAY DIFFRACTION (2.77 Å)