3MQ9

Crystal Structure of Ectodomain Mutant of BST-2/Tetherin/CD317 Fused to MBP

Summary for 3MQ9

• Entry DOI: 10.2210/pdb3mq9/pdb
• Related: 3MQ7 3MQB 3MQC
• Descriptor: Bone marrow stromal antigen 2 fused to Maltose-binding periplasmic protein (2 entities in total)
• Functional Keywords: hiv, antiviral protein
• Biological source: Escherichia coli (bacteria, human); More
• Cellular location: Golgi apparatus, trans-Golgi network: Q10589
• Total number of polymer chains: 8
• Total formula weight: 417547.41

Authors

Xiong, Y.,Yang, H.,Wang, J.,Meng, W. (deposition date: 2010-04-27, release date: 2010-10-27, Last modification date: 2024-10-30)

Primary citation

Yang, H.,Wang, J.,Jia, X.,McNatt, M.W.,Zang, T.,Pan, B.,Meng, W.,Wang, H.W.,Bieniasz, P.D.,Xiong, Y.
Structural insight into the mechanisms of enveloped virus tethering by tetherin.
Proc.Natl.Acad.Sci.USA, 107:18428-18432, 2010

PubMed Abstract: Tetherin/BST2 is a type-II membrane protein that inhibits the release of a range of enveloped viruses, including HIV-1. Here we report three crystal structures of human tetherin, including the full-length ectodomain, a triple cysteine mutant and an ectodomain truncation. These structures show that tetherin forms a continuous alpha helix encompassing almost the entire ectodomain. Tetherin helices dimerize into parallel coiled coils via interactions throughout the C-terminal portion of the ectodomain. A comparison of the multiple structures of the tetherin dimer reveals inherent constrained flexibility at two hinges positioned at residues A88 and G109. In the crystals, two tetherin ectodomain dimers associate into a tetramer by forming an antiparallel four-helix bundle at their N termini. However, mutagenesis studies suggest that the tetrametric form of tetherin, although potentially contributing to, is not essential for its antiviral activity. Nonetheless, the structural and chemical properties of the N terminus of the ectodomain are important for optimal tethering function. This study provides detailed insight into the mechanisms by which this broad-spectrum antiviral restriction factor can function.

PubMed: 20940320
DOI: 10.1073/pnas.1011485107

Experimental method

X-RAY DIFFRACTION (2.8 Å)