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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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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