M. Oblatt-Montal

TL;DR: The structures of functional peptides corresponding to the predicted channel-lining M2 segments of the nicotinic acetylcholine receptor and of a glutamate receptor of the NMDA subtype (NMDAR) were determined using solution NMR experiments on micelle samples, and solid-state N MR experiments on bilayer samples.

TL;DR: The ability of Vpu to increase virus release from infected cells may be correlated with an ion channel activity of the TM domain, thereby providing a potential target for drug intervention based on the development of VPU‐specific channel blockers.

TL;DR: The three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) of HIV-1 was determined by NMR spectroscopy in micelle and bilayer samples to determine the structural features of the ion-channel activity that may be associated with the protein's role in facilitating the budding of new virus particles from infected cells.

TL;DR: NMR experiments show that the pattern of channel activity is characteristic of the self-assembly of conductive oligomers in the membrane and is compatible with the structural and functional findings.

TL;DR: The assignment of backbone resonances enabled the secondary structure of the constructs corresponding to the transmembrane and the cytoplasmic domains of Vpu to be defined in micelle samples by solution NMR spectroscopy and demonstrated that the topology of the domains is retained in the truncated polypeptides.