Elusive envelope glycoproteins

Credit: © FELIX MÖCKEL" /> Credit: © FELIX MÖCKEL The paper: B. Chen et al., "Structure of an unliganded simian immunodeficiency virus gp120 core," Nature, 433:834-41, 2005. (Cited in 67 papers) The finding: Using X-ray crystallography, researchers at Harvard Medical School, led by Stephen Harrison, determined the structure, at 4 Å resolution, of the un-bound simian immunodeficiency virus envelope glycoprotein-gp120.

y Andrea Gawrylewski
Jan 31, 2007
<figcaption> Credit: © FELIX MÖCKEL</figcaption>
Credit: © FELIX MÖCKEL

The paper:

B. Chen et al., "Structure of an unliganded simian immunodeficiency virus gp120 core," Nature, 433:834-41, 2005. (Cited in 67 papers)

The finding:

Using X-ray crystallography, researchers at Harvard Medical School, led by Stephen Harrison, determined the structure, at 4 Å resolution, of the un-bound simian immunodeficiency virus envelope glycoprotein-gp120.

The surprise:

Harrison's team revealed striking conformational differences between gp120 unliganded and in interaction with the CD4 receptor. They also observed small "pocket" features on the protein that "fill up" when CD4 binding occurs-helping to explain why some small-molecule entry inhibitors are therapeutically successful.

The challenge:

The difficulty of growing unliganded SIV and HIV gp120 crystals continues to frustrate researchers, slowing the progress of getting a complete structure of the gp120/41 trimer, or "spike," according to Harrison.

The next step:

Viral therapies already include some small-molecule entry inhibitors that target the gp120-CD4 binding site....

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