ArticleBiochemistry2014
Recognition of the HIV capsid by the TRIM5α restriction factor is mediated by a subset of pre-existing conformations of the TRIM5α SPRY domain.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Restraint of Powassan virus replication by TRIM5α facilitates viral avoidance of antiviral immunity.bioRxiv : the preprint server for biology · 2026Article
- Indels allow antiviral proteins to evolve functional novelty inaccessible by missense mutations.Cell genomics · 2025Article
- Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025Review
- Indels allow antiviral proteins to evolve functional novelty inaccessible by missense mutations.bioRxiv : the preprint server for biology · 2024Article
- Clade-Specific Alterations within the HIV-1 Capsid Protein with Implications for Nuclear Translocation.Biomolecules · 2022Article
- Selection and identification of an RNA aptamer that specifically binds the HIV-1 capsid lattice and inhibits viral replication.Nucleic acids research · 2022Article
- Characterization of the primate TRIM gene family reveals the recent evolution in primates.Molecular genetics and genomics : MGG · 2020Article
- Article
- TRIM5α self-assembly and compartmentalization of the HIV-1 viral capsid.Nature communications · 2020Article
- Hierarchical assembly governs TRIM5α recognition of HIV-1 and retroviral capsids.Science advances · 2019Article
- Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019Review
- Not so unique to Primates: The independent adaptive evolution of TRIM5 in Lagomorpha lineage.PloS one · 2019Article
- The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5α.Journal of virology · 2018Article
- General Model for Retroviral Capsid Pattern Recognition by TRIM5 Proteins.Journal of virology · 2018Article
- The therapeutic landscape of HIV-1 via genome editing.AIDS research and therapy · 2017Review
- Dynamic conformational changes in the rhesus TRIM5α dimer dictate the potency of HIV-1 restriction.Virology · 2017Article
- Article
- Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5α.eLife · 2016Article
- Article
- Quarterly intrinsic disorder digest (January-February-March, 2014).Intrinsically disordered proteins · 2016Article
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2 authors.
Funding
Abstract
The binding of the TRIM5α restriction factor to the HIV capsid is mediated by the C-terminal SPRY domain of TRIM5α. Atomic-level details of this host-pathogen interaction, which involves mobile variable loops of the SPRY domain, remain unclear. Some of the key determinants of restriction are encompassed by the long and disordered v1 loop of the SPRY domain. We applied molecular modeling to elucidate the conformational repertoire of the v1 loop and its role in the interaction with the capsid. All-atom replica exchange molecular dynamics revealed multiple transient, interconverting states of the v1 loop consistent with the intrinsic disorder observed experimentally. The docking of the SPRY conformations representing 10 most populated states onto the high-resolution model of the assembled HIV-1 capsid revealed that a subset of v1 conformations produced plausible binding poses, in which the SPRY domain binds close to the pseudo-2-fold symmetry axis and the v1 loop spans the interhexamer gap. Such binding mode is well supported by the NMR binding data and known escape mutants. We speculate that the binding mode that involves interaction of the capsid with a subset of preexisting SPRY conformations arising from the intrinsic disorder of the v1 loop may explain the remarkable ability of TRIM5α to resist viral evasion by mutagenesis and to restrict divergent retroviruses.
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