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-Structure paper
Title | HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1. |
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Journal, issue, pages | J Virol, Vol. 87, Issue 12, Page 7191-7196, Year 2013 |
Publish date | Apr 17, 2013 |
Authors | Audray K Harris / Alberto Bartesaghi / Jacqueline L S Milne / Sriram Subramaniam / |
PubMed Abstract | We describe cryo-electron microscopic studies of the interaction between the ectodomain of the trimeric HIV-1 envelope glycoprotein (Env) and Z13e1, a broadly neutralizing antibody that targets the ...We describe cryo-electron microscopic studies of the interaction between the ectodomain of the trimeric HIV-1 envelope glycoprotein (Env) and Z13e1, a broadly neutralizing antibody that targets the membrane-proximal external region (MPER) of the gp41 subunit. We show that Z13e1-bound Env displays an open quaternary conformation similar to the CD4-bound conformation. Our results support the idea that MPER-directed antibodies, such as Z13e1, block viral entry by interacting with Env at a step after CD4 activation. |
External links | J Virol / PubMed:23596305 / PubMed Central |
Methods | EM (single particle) |
Resolution | 18.5 Å |
Structure data | EMDB-5680: |
Source |
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