24 February 2005
HIV turncoat: gp120 unbound
The structure of the gp120 envelope protein from HIV (human immunodeficiency virus) bound to the CD4 receptor from the host cell has been known since 1998, but its structure prior to receptor binding had remained elusive. At last unliganded gp120 from simian immunodeficiency virus has been successfully crystallized, and its structure determined to 4 Å resolution. The protein's shape is very different in bound and unbound states: this large-scale structural change may be part of the subterfuge used by gp120 to evade the host's immune system. In addition a probable binding site for the recently discovered drug-candidate BMS-378806 was identified. BMS-378806 and some of its analogues are candidate antiretrovirals that inhibit the entry of HIV-1 into host cells by blocking CD4 binding.
Structure of an unliganded simian immunodeficiency virus gp120 core
BING CHEN, ERIK M. VOGAN, HAIYUN GONG, JOHN J. SKEHEL, DON C. WILEY & STEPHEN C. HARRISON
Nature 433, 834–841 (2005); doi:10.1038/nature03327
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Human immunodeficiency virus: Refolding the envelope
PETER D. KWONG
HIV has evolved to avoid neutralization by human antibodies. New atomic-level details reveal that such evasion involves substantial refolding of its exterior glycoprotein.
Nature 433, 815–816 (2005); doi:10.1038/433815a
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