Structural model for the hexameric VPS4 ring, an ATPase required for HIV budding. VPS4 disassembles the machinery of the ESCRT pathway, which functions directly in viral budding. VPS4 appears to unfold protein substrates by pulling them through the narrow central pore structure (highlighted in orange).

This work is part of an ongoing collaboration between the Sundquist and Hill laboratories (Scott et al. EMBO J. (2005) 24, 3658-69).

The flexible conformations of Uro'gen III Synthase.

The crystal structure of the complex between Ubiquitin and the UEV domain of TSG101, a protein complex implicated in HIV transport and targeting to the cell surface.

Proteasome-activator complex.

Overview of the active site of the 5N-Gln.

The active site of the 5N-Gln Methyltransferase involved in Ribosomal Release Factor methylation, a crucial step in proper efficiency of amino-peptide release from the ribosome. The electron density maps prove the presence of a partially methylated gln reside in the active site, the S-adenosylmethionine/Homocystein substrate is in yellow, protein in green.

Hylogeny of ADARs - Bass Lab.