| Literature DB >> 20399176 |
Andreas Hinz1, Nolwenn Miguet1, Ganesh Natrajan1, Yoshiko Usami2, Hikaru Yamanaka2, Patricia Renesto1, Bettina Hartlieb1, Andrew A McCarthy3, Jean-Pierre Simorre4, Heinrich Göttlinger2, Winfried Weissenhorn5.
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. Copyright 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID： 20399176 PMCID： PMC2859121 DOI： 10.1016/j.chom.2010.03.005
Source DB: PubMed Journal: Cell Host Microbe ISSN： 1931-3128 Impact factor: 21.023