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Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function
Open accessAbstract
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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“The SPRY domain of TRIM21, a major autoantigen in autoimmune diseases, was solved in complex with the Fc region of the immunoglobulin IgG 126 , revealing a well-defined pocket at the IgG binding site”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [126]
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Cites
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Casciola-Rosen, L. A., Anhalt, G. J., & Rosen, A. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.179.4.1317 · Cited by 1,723
Likelihood-enhanced fast translation functions
McCoy, A. J., Grosse‐Kunstleve, R. W., Storoni, L. C., & Read, R. J. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905001617 · Cited by 1,641
The International FMF Consortium (1997) · Cell · doi:10.1016/s0092-8674(00)80539-5 · Cited by 1,550
Deisenhofer, J. (1981) · Biochemistry · doi:10.1021/bi00512a001 · Cited by 1,539
Deisenhofer, J. (1981) · PubMed · Cited by 1,422
SMART 5: domains in the context of genomes and networks
Letunić, I. (2005) · Nucleic Acids Research · doi:10.1093/nar/gkj079 · Cited by 983
TRIM family proteins: retroviral restriction and antiviral defence
Nisole, S., Stoye, J. P., & Saïb, A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1248 · Cited by 761
Stremlau, M. H., Perron, M. J., Lee, M. N., Li, Y., Song, B., Javanbakht, H., Diaz‐Griffero, F., Anderson, D. J., Sundquist, W. I., & Sodroski, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509996103 · Cited by 736
Antibody Multispecificity Mediated by Conformational Diversity
James, L. C., Roversi, P., & Tawfik, D. S. (2003) · Science · doi:10.1126/science.1079731 · Cited by 719
Self-citation
Research works printed but not linked: 2
- DP McCauliffe , L Wang , M Satoh , WH Reeves , D Small J Rheumatol 24 , 860–866 (1997).
- MB Frank , K Itoh , A Fujisaku , P Pontarotti , MG Mattei , BR Neas Am J Hum Genet 52 , 183–191 (1993).
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Yoshimi, R., Chang, T.-H., Wang, H., Atsumi, T., Morse, H. C., & Ozato, K. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804121 · Cited by 156
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Self-citationDong, W., Wei, X., Zhang, F., Hao, J., Huang, F., Zhang, C., & Liang, W. P. (2014) · Scientific Reports · doi:10.1038/srep07237 · Cited by 104
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Metadata
- 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)
- 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
- 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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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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