ArticleProceedings of the National Academy of Sciences of the United States of America1999
Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed, 211 citations in OpenAlex.
- The Assembly of HTLV-1-How Does It Differ from HIV-1?Viruses · 2024Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- High-Risk Mucosal Human Papillomavirus 16 (HPV16) E6 Protein and Cutaneous HPV5 and HPV8 E6 Proteins Employ Distinct Strategies To Interfere with Interferon Regulatory Factor 3-Mediated Beta Interferon Expression.Journal of virology · 2022Article
- A bioactive phlebovirus-like envelope protein in a hookworm endogenous virus.Science advances · 2022Article
- Differential recognition of canonical NF-κB dimers by Importin α3.Nature communications · 2022Article
- The Past, Present, and Future of a Human T-Cell Leukemia Virus Type 1 Vaccine.Frontiers in microbiology · 2022Review
- Novel Genetic Constructs for Production of Recombinant HTLV-1/2 Antigens and Evaluation of Their Reactivity to Plasma Samples from HTLV-1-Infected Patients.Journal of clinical microbiology · 2021Article
- Improved Methods for Preparing the Telomere Tethering Complex Bqt1-Bqt2 for Structural Studies.The protein journal · 2020Article
- Passenger sequences can promote interlaced dimers in a common variant of the maltose-binding protein.Scientific reports · 2019Article
- X-ray Structures of the Post-fusion 6-Helix Bundle of the Human Syncytins and their Functional Implications.Journal of molecular biology · 2019Article
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- T4 lysozyme-facilitated crystallization of the human molybdenum cofactor-dependent enzyme mARC.Acta crystallographica. Section F, Structural biology communications · 2018Article
- The HTLV-1 gp21 fusion peptide inhibits antigen specific T-cell activation in-vitro and in mice.PLoS pathogens · 2018Article
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- Article
- The macro domain as fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2017Article
- Design of an expression system to enhance MBP-mediated crystallization.Scientific reports · 2017Article
- Protein crystallization: Eluding the bottleneck of X-ray crystallography.AIMS biophysics · 2017Article
- Pentameric quaternary structure of the intracellular domain of serotonin type 3A receptors.Scientific reports · 2016Article
- Crystal structures of MBP fusion proteins.Protein science : a publication of the Protein Society · 2016Review
45 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Retroviral entry into cells depends on envelope glycoproteins, whereby receptor binding to the surface-exposed subunit triggers membrane fusion by the transmembrane protein (TM) subunit. We determined the crystal structure at 2.5-A resolution of the ectodomain of gp21, the TM from human T cell leukemia virus type 1. The gp21 fragment was crystallized as a maltose-binding protein chimera, and the maltose-binding protein domain was used to solve the initial phases by the method of molecular replacement. The structure of gp21 comprises an N-terminal trimeric coiled coil, an adjacent disulfide-bonded loop that stabilizes a chain reversal, and a C-terminal sequence structurally distinct from HIV type 1/simian immunodeficiency virus gp41 that packs against the coil in an extended antiparallel fashion. Comparison of the gp21 structure with the structures of other retroviral TMs contrasts the conserved nature of the coiled coil-forming region and adjacent disulfide-bonded loop with the variable nature of the C-terminal ectodomain segment. The structure points to these features having evolved to enable the dual roles of retroviral TMs: conserved fusion function and an ability to anchor diverse surface-exposed subunit structures to the virion envelope and infected cell surface. The structure of gp21 implies that the N-terminal fusion peptide is in close proximity to the C-terminal transmembrane domain and likely represents a postfusion conformation.
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