Structural basis for tetherin antagonism as a barrier to zoonotic lentiviral transmission
C. Z. Buffalo, C. Sturzel, E. Heusinger, D. Kmiec, F. Kirchhoff, J. Hurley, X. Ren
The paper determines the structure of SIV Nef interacting with simian tetherin and AP-2, revealing how Nef bypasses tetherin's antiviral function by refolding AP-2 and creating a binding site for the DIWK motif.
bioRxiv · May 17, 2019Biochemistry