ArticleProceedings of the National Academy of Sciences of the United States of America2008
TRIM21 is an IgG receptor that is structurally, thermodynamically, and kinetically conserved.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.
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Who cites it
124 citing papers in PubMed, 197 citations in OpenAlex.
- Capsid-Targeting Biologic Achieves Broad HIV-1 Neutralization with a High Barrier to Resistance.International journal of molecular sciences · 2026Article
- HBO1 suppresses anti-tumor immunity of CD8⁺ T Cells in thyroid cancer by recruiting BRD4 to regulate VTCN1 expression.Cancer immunology, immunotherapy : CII · 2026Article
- Anti-capsid nanobodies function as HIV-1 capsid inhibitors by intracellular capsid degradation.Communications biology · 2026Article
- Redirecting TRIM21 with TRIMTACs for the targeted degradation of multimeric proteins.The FEBS journal · 2026Review
- Tripartite motif containing 21 autoimmunity primes CD8Arthritis research & therapy · 2026Article
- The molecular basis for nuclear pore destruction by a proximity-inducing molecular glue.Cell chemical biology · 2026Article
- TRIM21 is a molecular rheostat for influenza A virus replication.bioRxiv : the preprint server for biology · 2026Article
- Identification of a Highly Potent Neutralizing Nanobody Against Human Adenovirus Type 4.Vaccines · 2025Article
- A replicating RNA vaccine protects against severe fever with thrombocytopenia syndrome virus infection in mice.NPJ vaccines · 2025Article
- Crystallographic fragment screening reveals ligand hotspots in TRIM21 PRY-SPRY domain.Communications chemistry · 2025Article
- FcRn-dependent IgG accumulation in adipose tissue unmasks obesity pathophysiology.Cell metabolism · 2025Article
- LOPAC library screening identifies suramin as a TRIM21 binder with a unique binding mode revealed by crystal structure.Acta crystallographica. Section F, Structural biology communications · 2025Article
- TRIM21 regulation of IRF-mediated type I interferon signaling in systemic autoimmune diseases.Frontiers in immunology · 2025Review
- Antibodies targeting the Crimean-Congo Hemorrhagic Fever Virus nucleoprotein protect via TRIM21.Nature communications · 2024Article
- ZnBalkan medical journal · 2024Article
- FAT10 inhibits TRIM21 to down-regulate antiviral type-I interferon secretion.Life science alliance · 2024Article
- Remodeling of anti-tumor immunity with antibodies targeting a p53 mutant.Journal of hematology & oncology · 2024Article
- TRIM21 is critical in regulating hepatocellular carcinoma growth and response to therapy by altering the MST1/YAP pathway.Cancer science · 2024Article
- Non-proteolytic ubiquitination of HBx controls HBV replication.Virologica Sinica · 2024Article
- Fatty acid synthase (FASN) signalome: A molecular guide for precision oncology.Molecular oncology · 2024Article
64 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The newly identified tripartite motif (TRIM) family of proteins mediate innate immunity and other critical cellular functions. Here we show that TRIM21, which mediates the autoimmune diseases rheumatoid arthritis, systemic lupus erythematosus, and Sjögren's syndrome, is a previously undescribed IgG receptor with a binding mechanism unlike known mammalian Fcgamma receptors. TRIM21 simultaneously targets conserved hot-spot residues on both Ig domains of the Fc fragment using a PRYSPRY domain with a preformed multisite interface. The binding sites on both TRIM21 and Fc are highly conserved to the extent that the proteins are functionally interchangeable through murine, canine, primate, and human species. Pre-steady-state analysis exposes mechanistic conservation at the level of individual residues, which make the same energetic and kinetic contributions to binding despite varying in sequence. Together, our results reveal that TRIM21 is a previously undescribed type of IgG receptor based on a non-Ig scaffold whose interaction at the fundamental level-structural, thermodynamic, and kinetic-is evolutionarily conserved.
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Registered trials
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.