Structural Studies of Computationally Designed Inhibitors of HIV Gp41

Authors

Abi Paudel, University of Nebraksa LIncolnFollow
Peter Madzelan, University of Nebraska LincolnFollow
William J. Allen, SUNY Stony Brook
Robert C. Rizzo, SUNY Stony Brook
Mark A. Wilson, University of Nebraska, LincolnFollow

Date of this Version

4-2016

Document Type

Poster

Citation

UCARE Poster session, University of Nebraska-Lincoln Research Fair, April 2016, Lincoln, NE.

Comments

Copyright © 2016 Abi Paudel, Peter Madzelan, William J. Allen ,Robert C. Rizzo, Mark A. Wilson

Abstract

Human immunodeficiency virus (HIV) infection is a major public health concern. New strategies that target viral entry hold promise for preventing infection or for enhancing the efficacy of existing anti-retroviral therapy. We have targeted the HIV protein gp41, required for initial membrane fusion and viral entry, for computational lead compound development and structural characterization. We have successfully purified an engineered version of this protein (gp41-5) that has an exposed patch that resembles the pre-fusion complex that is presumed to be an important intermediate in fusion. We crystallized this protein and collected a complete data set, however the crystals suffer from an unusual order-disorder pathology. Current work is identifying improved crystallization conditions that will allow determination of the crystal structure of gp41-5 with computationally identified compounds that inhibit viral entry.