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TitleSubunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer.
Journal, issue, pagesNat Struct Mol Biol, Vol. 19, Issue 9, Page 893-899, Year 2012
Publish dateAug 5, 2012
AuthorsYoudong Mao / Liping Wang / Christopher Gu / Alon Herschhorn / Shi-Hua Xiang / Hillel Haim / Xinzhen Yang / Joseph Sodroski /
PubMed AbstractThe trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) spike is a molecular machine that mediates virus entry into host cells and is the sole target for virus- ...The trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) spike is a molecular machine that mediates virus entry into host cells and is the sole target for virus-neutralizing antibodies. The mature Env spike results from cleavage of a trimeric glycoprotein precursor, gp160, into three gp120 and three gp41 subunits. Here, we describe an ~11-Å cryo-EM structure of the trimeric HIV-1 Env precursor in its unliganded state. The three gp120 and three gp41 subunits form a cage-like structure with an interior void surrounding the trimer axis. Interprotomer contacts are limited to the gp41 transmembrane region, the torus-like gp41 ectodomain and a trimer-association domain of gp120 composed of the V1, V2 and V3 variable regions. The cage-like architecture, which is unique among characterized viral envelope proteins, restricts antibody access, reflecting requirements imposed by HIV-1 persistence in the host.
External linksNat Struct Mol Biol / PubMed:22864288 / PubMed Central
MethodsEM (single particle)
Resolution10.8 Å
Structure data

EMDB-5418:
Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
Method: EM (single particle) / Resolution: 10.8 Å

Source
  • Human immunodeficiency virus 1

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