Crystal structures of the HIV-1 inhibitory cyanobacterial protein MVL free and bound to Man3GlcNAc2: structural basis for specificity and high-affinity binding to the core pentasaccharide from n-linked oligomannoside.

@article{Williams2005CrystalSO,
  title={Crystal structures of the HIV-1 inhibitory cyanobacterial protein MVL free and bound to Man3GlcNAc2: structural basis for specificity and high-affinity binding to the core pentasaccharide from n-linked oligomannoside.},
  author={David A Williams and Jae Young Lee and Mengli Cai and Carole A Bewley and G Marius Clore},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 32},
  pages={29269-76}
}
The cyanobacterial protein MVL inhibits HIV-1 envelope-mediated cell fusion at nanomolar concentrations by binding to high mannose N-linked carbohydrate on the surface of the envelope glycoprotein gp120. Although a number of other carbohydrate-binding proteins have been shown to inhibit HIV-1 envelope-mediated cell fusion, the specificity of MVL is unique in that its minimal target comprises the Man(alpha)(1-->6)Man(beta)(1-->4)GlcNAc(beta)(1-->4)GlcNAc tetrasaccharide core of oligomannosides… CONTINUE READING

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Acta Crystallogr

A. T. Brünger, D. Adams.P., +11 authors G. L. Warren
Sect . A • 1991

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