Cited by 386Monoclonal and Polyclonal Antibodies ResearchInflammasome and immune disordersEnzyme Structure and Function

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Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function

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James, Leo C., Keeble, Anthony H., Khan, Zahra, Rhodes, David A., Trowsdale, John·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0609174104PMC PMC1851072

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Abstract

The human tripartite motif (TRIM) family comprises 70 members, including HIV restriction factor TRIM5α and disease-associated proteins TRIM20 (pyrin) and TRIM21. TRIM proteins have conserved domain architecture but diverse cellular roles. Here, we describe how the C-terminal PRYSPRY domain mediates diverse TRIM functions. The crystal structure of TRIM21 PRYSPRY in complex with its target IgG Fc reveals a canonical binding interface comprised of two discrete pockets formed by antibody-like variable loops. Alanine scanning of this interface has identified the hot-spot residues that control TRIM21 binding to Fc; the same hot-spots control HIV/murine leukemia virus restriction by TRIM5α and mediate severe familial Mediterranean fever in TRIM20/pyrin. Characterization of the IgG binding site for TRIM21 PRYSPRY reveals TRIM21 as a superantigen analogous to bacterial protein A and suggests that an antibody bipolar bridging mechanism may contribute to the pathogenic accumulation of anti-TRIM21 autoantibody immune complex in autoimmune disease.

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Additional file 1 of TRIM36 inhibits tumorigenesis through the Wnt/β-catenin pathway and promotes caspase-dependent apoptosis in hepatocellular carcinoma
Tong, Q., Yi, M., Kong, P., Xu, L., Huang, W., Niu, Y., Gan, X., Zhan, H., Tian, R., & Yan, D. (2022) · Figshare · doi:10.6084/m9.figshare.21009594
Additional file 5 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
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Additional file 6 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26746874
Additional file 1 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26211458
Additional file 4 of TRIM36 inhibits tumorigenesis through the Wnt/β-catenin pathway and promotes caspase-dependent apoptosis in hepatocellular carcinoma
Tong, Q., Yi, M., Kong, P., Xu, L., Huang, W., Niu, Y., Gan, X., Zhan, H., Tian, R., & Yan, D. (2022) · Figshare · doi:10.6084/m9.figshare.21009606
Additional file 9 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26746883
Additional file 3 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26746865
Additional file 7 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26746877
Additional file 8 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26746880
Additional file 2 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26211678
Additional file 4 of An investigation of the molecular characterization of the tripartite motif (TRIM) family and primary validation of TRIM31 in gastric cancer
Ding, Y., Lu, Y., Guo, J., Chen, S., Han, X., Wang, S., Zhang, M., Wang, R., Song, J., Wang, K., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26746868
Additional file 3 of TRIM36 inhibits tumorigenesis through the Wnt/β-catenin pathway and promotes caspase-dependent apoptosis in hepatocellular carcinoma
Tong, Q., Yi, M., Kong, P., Xu, L., Huang, W., Niu, Y., Gan, X., Zhan, H., Tian, R., & Yan, D. (2022) · Figshare · doi:10.6084/m9.figshare.21009600
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Chung, C., Zhao, Q., & Pinal‐Fernandez, I. (2026) · Current Opinion in Rheumatology · doi:10.1097/bor.0000000000001196
TRIM21 Neutralizes Hazara Virus Using a Dual Mechanism of Nucleoprotein Caging and Ubiquitination
Jahun, A. S., Vamos, B., Albecka, A., Vaysburd, M., Hawman, D. W., & James, L. C. (2026) · Viruses · doi:10.3390/v18090974
Self-citation
Mammalian TRIM21 Exhibits Gene-Wide Episodic Diversifying Selection with Statistically Supported and Structurally Positioned Evolutionary Candidate ResiduesPreprint
NEELKANTAN, H. J. (2026) · Research Square · doi:10.21203/rs.3.rs-11209229/v1
BindingDB Entry 50020885: Discovery of Ligands for TRIM58, a Novel Tissue-Selective E3 Ligase.
BindingDB (2024) · UC San Diego · doi:10.7270/q2fr023d

Authors: James, L. C., Keeble, A. H., Khan, Z., Rhodes, D. A., & Trowsdale, J.
Affiliations: MRC Laboratory of Molecular Biology (GB)
University of Cambridge (GB)
ORCID: James, Leo C.
Keeble, Anthony H.
Rhodes, David A.
Trowsdale, John
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2007-04-10
Volume: 104
Issue: 15
Pages: 6200-6205
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0609174104
PMC: PMC1851072
OpenAlex: W2022754521
Cited by: 386
References: 50
Citations by year: 2026: 20 · 2025: 26 · 2024: 27 · 2023: 25 · 2022: 22 · 2021: 24 · 2020: 26 · 2019: 27 · 2018: 11 · 2017: 18 · 2016: 17 · 2015: 15 · 2014: 19 · 2013: 19 · 2012: 18
FWCI: 13.29
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
Medical Research Council
Topics: Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: tripartite motif proteins, PRYSPRY domain, TRIM21, TRIM5α, IgG Fc binding, protein crystal structure, familial Mediterranean fever, superantigens, autoantibodies, immune complexes, autoimmune disease, protein-protein interaction
MeSH terms: SS-A Antigen, Amino Acid Sequence, Autoantibodies, Autoimmune Diseases, Binding Sites, Antibody, Calorimetry, Cell Line, Crystallography, DNA-Binding Proteins, Fluorescence Polarization, Multigene Family, Humans, Immunoglobulin G, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Protein Conformation, Ribonucleoproteins, Structure-Activity Relationship, Gene Expression, Sequence Alignment, Protein Structure, Tertiary

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Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function

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