Ontology highlight
ABSTRACT:
SUBMITTER: Skasko M
PROVIDER: S-EPMC3249111 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Skasko Mark M Wang Yan Y Tian Ye Y Tokarev Andrey A Munguia Jason J Ruiz Autumn A Stephens Edward B EB Opella Stanley J SJ Guatelli John J
The Journal of biological chemistry 20111109 1
The Vpu protein of HIV-1 antagonizes BST-2 (tetherin), a broad spectrum effector of the innate immune response to viral infection, by an intermolecular interaction that maps genetically to the α-helical transmembrane domains (TMDs) of each protein. Here we utilize NMR spectroscopy to describe key features of the helix-helix pairing that underlies this interaction. The antagonism of BST-2 involves a sequence of three alanines and a tryptophan spaced at four residue intervals within the Vpu TMD he ...[more]