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-Structure paper
Title | A bipartite structural organization defines the SERINC family of HIV-1 restriction factors. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 27, Issue 1, Page 78-83, Year 2020 |
Publish date | Jan 6, 2020 |
Authors | Valerie E Pye / Annachiara Rosa / Cinzia Bertelli / Weston B Struwe / Sarah L Maslen / Robin Corey / Idlir Liko / Mark Hassall / Giada Mattiuzzo / Allison Ballandras-Colas / Andrea Nans / Yasuhiro Takeuchi / Phillip J Stansfeld / J Mark Skehel / Carol V Robinson / Massimo Pizzato / Peter Cherepanov / |
PubMed Abstract | The human integral membrane protein SERINC5 potently restricts HIV-1 infectivity and sensitizes the virus to antibody-mediated neutralization. Here, using cryo-EM, we determine the structures of ...The human integral membrane protein SERINC5 potently restricts HIV-1 infectivity and sensitizes the virus to antibody-mediated neutralization. Here, using cryo-EM, we determine the structures of human SERINC5 and its orthologue from Drosophila melanogaster at subnanometer and near-atomic resolution, respectively. The structures reveal a novel fold comprised of ten transmembrane helices organized into two subdomains and bisected by a long diagonal helix. A lipid binding groove and clusters of conserved residues highlight potential functional sites. A structure-based mutagenesis scan identified surface-exposed regions and the interface between the subdomains of SERINC5 as critical for HIV-1-restriction activity. The same regions are also important for viral sensitization to neutralizing antibodies, directly linking the antiviral activity of SERINC5 with remodeling of the HIV-1 envelope glycoprotein. |
External links | Nat Struct Mol Biol / PubMed:31907454 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.33 - 8.2 Å |
Structure data | EMDB-10277: EMDB-10279, PDB-6sp2: |
Chemicals | ChemComp-LMN: ChemComp-P5S: ChemComp-CDL: |
Source |
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Keywords | MEMBRANE PROTEIN / Anti-retroviral / TM10 / SERINC fold / novel fold |