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Quaternary contact in the initial interaction of CD4 with the HIV-1 envelope trimer.

Nat. Struct. Mol. Biol.. 2017; 
Liu Qingbo,Acharya Priyamvada,Dolan Michael A,Zhang Peng,Guzzo Christina,Lu Jacky,Kwon Alice,Gururani Deepali,Miao Huiyi,Bylund Tatsiana,Chuang Gwo-Yu,Druz Aliaksandr,Zhou Tongqing,Rice William J,Wigge Christoph,Carragher Bridget,Potter Clinton S,Kwong Peter D,Lusso P
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Recombinant Proteins for trimers (GenScript; A00174). Monomeric gp120s or trimers were captured on the plates, and various Get A Quote

摘要

Binding of the gp120 envelope (Env) glycoprotein to the CD4 receptor is the first step in the HIV-1 infectious cycle. Although the CD4-binding site has been extensively characterized, the initial receptor interaction has been difficult to study because of major CD4-induced structural rearrangements. Here we used cryogenic electron microscopy (cryo-EM) to visualize the initial contact of CD4 with the HIV-1 Env trimer at 6.8-? resolution. A single CD4 molecule is embraced by a quaternary HIV-1-Env surface formed by coalescence of the previously defined CD4-contact region with a second CD4-binding site (CD4-BS2) in the inner domain of a neighboring gp120 protomer. Disruption of CD4-BS2 destabilized CD4-trimer in... More

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