ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 108 citations in OpenAlex.
- Ubiquitin E3 ligase activity in TRIpartite Motif (TRIM) family proteins.Biochemical Society transactions · 2026Review
- Study of retroviral restrictions in a Tadarida bat cell line enlightens specific early blocks and TRIM5 locus multiplication.Journal of virology · 2026Article
- Restraint of Powassan virus replication by TRIM5α facilitates viral avoidance of antiviral immunity.bioRxiv : the preprint server for biology · 2026Article
- Insights into the membrane repair mechanism by the coiled-coil-mediated oligomerization of TRIM72.Biochemistry and biophysics reports · 2025Article
- Probing the molecular determinants of Ty1 retrotransposon restriction specificity in yeast.PLoS genetics · 2025Article
- Mesoscale regulation of microtubule-organizing centers by the E3 ligase TRIM37.Nature structural & molecular biology · 2025Article
- Endogenous Retroviruses in Host-Virus Coevolution: From Genomic Domestication to Functional Innovation.Genes · 2025Review
- Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025Review
- Molecular Determinants of PQBP1 Binding to the HIV-1 Capsid Lattice.Journal of molecular biology · 2024Article
- Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane.Nature structural & molecular biology · 2023Article
- TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions.Computational and structural biotechnology journal · 2023Article
- Structural and functional asymmetry of RING trimerization controls priming and extension events in TRIM5α autoubiquitylation.Nature communications · 2022Article
- Mapping the interaction between Trim28 and the KRAB domain at the center of Trim28 silencing of endogenous retroviruses.Protein science : a publication of the Protein Society · 2022Article
- The B-box1 domain of PML mediates SUMO E2-E3 complex formation through an atypical interaction with UBC9.Biophysical chemistry · 2022Article
- Mapping of molecular interactions between human E3 ligase TRIM69 and Dengue virus NS3 protease using hydrogen-deuterium exchange mass spectrometry.Cellular and molecular life sciences : CMLS · 2022Article
- Structural studies of the coiled-coil domain of TRIM75 reveal a tetramer architecture facilitating its E3 ligase complex.Computational and structural biotechnology journal · 2022Article
- HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules.Retrovirology · 2021Review
- Structure of a Ty1 restriction factor reveals the molecular basis of transposition copy number control.Nature communications · 2021Article
- Human TRIM5α senses and restricts LINE-1 elements.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Duplication and divergence of the retrovirus restriction gene Fv1 in Mus caroli allows protection from multiple retroviruses.PLoS genetics · 2020Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
Restriction factors (RFs) form important components of host defenses to retroviral infection. The Fv1, Trim5α, and TrimCyp RFs contain N-terminal dimerization and C-terminal specificity domains that target assembled retroviral capsid (CA) proteins enclosing the viral core. However, the molecular detail of the interaction between RFs and their CA targets is unknown. Therefore, we have determined the crystal structure of the B-box and coiled-coil (BCC) region from Trim5α and used small-angle X-ray scattering to examine the solution structure of Trim5α BCC, the dimerization domain of Fv1 (Fv1Ntd), and the hybrid restriction factor Fv1Cyp comprising Fv1NtD fused to the HIV-1 binding protein Cyclophilin A (CypA). These data reveal that coiled-coil regions of Fv1 and Trim5α form extended antiparallel dimers. In Fv1Cyp, two CypA moieties are located at opposing ends, creating a molecule with a dumbbell appearance. In Trim5α, the B-boxes are located at either end of the coiled-coil, held in place by interactions with a helical motif from the L2 region of the opposing monomer. A comparative analysis of Fv1Cyp and CypA binding to a preformed HIV-1 CA lattice reveals how RF dimerization enhances the affinity of interaction through avidity effects. We conclude that the antiparallel organization of the NtD regions of Fv1 and Trim5α dimers correctly positions C-terminal specificity and N-terminal effector domains and facilitates stable binding to adjacent CA hexamers in viral cores.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.