Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer | Zendy

Jeong Hyun Lee | Zendy; Gabriel Ozorowski | Zendy; Andrew B. Ward | Zendy

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Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer

Author(s) -

Jeong Hyun Lee,

Gabriel Ozorowski,

Andrew B. Ward

Publication year - 2016

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aad2450

Subject(s) - trimer , glycoprotein , human immunodeficiency virus (hiv) , viral envelope , envelope (radar) , cryo electron microscopy , chemistry , gp41 , cytoplasm , protein structure , viral protein , antibody , virology , biophysics , viral entry , biology , biochemistry , viral replication , virus , epitope , computer science , genetics , telecommunications , dimer , radar , organic chemistry

A more complete look at the HIV-1 envelope HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Leeet al. used cryo–electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts.Science , this issue p.1043

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