ReviewProtein science : a publication of the Protein Society2013
Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity.
Review in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed.
- Trial
- Article
- Tripartite motif-containing 34 (TRIM34) protein interacts with the nucleocytoplasmic transport machinery and negatively modulates antiviral responses.PLoS pathogens · 2026Article
- Phenotypic prediction of missense variants via deep contrastive learning.Nature biomedical engineering · 2026Article
- Characterization of Lysine Methylation During Neuronal Differentiation of LUHMES cells.bioRxiv : the preprint server for biology · 2026Article
- TRIM proteins as emerging regulators of immune pathways: potential therapeutic targets in immune-related disorders.Frontiers in immunology · 2026Review
- Structural analysis of TRIM family PRYSPRY domains and its implications for E3-ligand design.Journal of structural biology: X · 2025Article
- Molecular mechanisms and regulation of inflammasome activation and signaling: sensing of pathogens and damage molecular patterns.Cellular & molecular immunology · 2025Review
- Review
- A Brief Molecular History of Vγ9Vδ2 TCR-Mediated Phosphoantigen Sensing.Immunological reviews · 2025Review
- Cytokine Receptor-like Factor 3 (CRLF3) and Its Emerging Roles in Neurobiology, Hematopoiesis and Related Human Diseases.International journal of molecular sciences · 2025Review
- Domain-Shuffling in the Evolution of Cyclostomes and Gnathostomes.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2025Article
- Therapeutic potential of TRIM family proteins in gastric cancer: from signaling pathway regulation to precision targeting strategies.Frontiers in oncology · 2025Review
- Heterozygous BTNL8 variants in individuals with multisystem inflammatory syndrome in children (MIS-C).The Journal of experimental medicine · 2024Article
- Emerging roles of tripartite motif family proteins (TRIMs) in breast cancer.Cancer medicine · 2024Review
- Genome-wide association study for stayability at different calvings in Nellore beef cattle.BMC genomics · 2024Article
- Exploring the Mechanisms, Biomarkers, and Therapeutic Targets of TRIM Family in Gastrointestinal Cancer.Drug design, development and therapy · 2024Review
- A Ménage à trois: NLRC5, immunity, and metabolism.Frontiers in immunology · 2024Review
- adgrl3.1-deficient zebrafish show noradrenaline-mediated externalizing behaviors, and altered expression of externalizing disorder-candidate genes, suggesting functional targets for treatment.Translational psychiatry · 2023Article
- Article
11 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SPRY domain is a protein interaction module found in 77 murine and ~100 human proteins, and is implicated in important biological pathways, including those that regulate innate and adaptive immunity. The current definition of the SPRY domain is based on a sequence repeat discovered in the splA kinase and ryanodine receptors. The greater SPRY family is divided into the B30.2 (which contains a PRY extension at the N-terminus) and "SPRY-only" sub-families. In this brief review, we examine the current structural and biochemical literature on SPRY/B30.2 domain involvement in key immune processes and highlight a PRY-like 60 amino acid region in the N-terminus of "SPRY-only" proteins. Phylogenetic, structural, and functional analyses suggest that this N-terminal region is related to the PRY region of B30.2 and should be characterized as part of an extended SPRY domain. Greater understanding of the functional importance of the N-terminal region in "SPRY only" proteins will enhance our ability to interrogate SPRY interactions with their respective binding partners.
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