ArticleLife science alliance2020
Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold.
Article in Life science alliance, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Multiomic characterization of DNA released after airway exposure to allergens and nanoparticles reveals selective export of repetitive and fragile site DNA.Physiological genomics · 2026Article
- From infection to invasion: The role of deleted in malignant brain tumors 1 inWorld journal of clinical oncology · 2025Article
- Structural elucidation of the haptoglobin-hemoglobin clearance mechanism by macrophage scavenger receptor CD163.PLoS biology · 2025Article
- Review
- The Cryo-EM structure of human CD163 bound to haptoglobin-hemoglobin reveals molecular mechanisms of hemoglobin scavenging.Nature communications · 2024Article
- Cryo-EM reveals structural basis for human AIM/CD5L recognition of polymeric immunoglobulin M.Nature communications · 2024Article
- CD5L associates with IgM via the J chain.Nature communications · 2024Article
- Refolding, Crystallization, and Crystal Structure Analysis of a Scavenger Receptor Cysteine-Rich Domain of Human Salivary Agglutinin Expressed in Escherichia coli.The protein journal · 2024Article
- Genome-Wide Comparative Analysis of SRCR Gene Superfamily in Invertebrates Reveals Massive and Independent Gene Expansions in the Sponge and Sea Urchin.International journal of molecular sciences · 2024Article
- Salivary microbiome changes distinguish response to chemoradiotherapy in patients with oral cancer.Microbiome · 2023Article
- LOXL2 in Cancer: A Two-Decade Perspective.International journal of molecular sciences · 2023Review
- New Functions of Intracellular LOXL2: Modulation of RNA-Binding Proteins.Molecules (Basel, Switzerland) · 2023Article
- Review
- Effects of equine SALSA on neutrophil phagocytosis and macrophage cytokine production.PloS one · 2022Article
- Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.Acta crystallographica. Section D, Structural biology · 2021Article
- Interactions of ferritin with scavenger receptor class A members.The Journal of biological chemistry · 2020Article
- Why the lower reported prevalence of asthma in patients diagnosed with COVID-19 validates repurposing EDTA solutions to prevent and manage treat COVID-19 disease.Medical hypotheses · 2020Article
- Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins.Frontiers in microbiology · 2020Review
- Dissecting the Extracellular Complexity of Neuromuscular Junction Organizers.Frontiers in molecular biosciences · 2019Review
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Authors and funding
4 authors.
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Abstract
The scavenger receptor cysteine-rich (SRCR) family of proteins comprises more than 20 membrane-associated and secreted molecules. Characterised by the presence of one or more copies of the ∼110 amino-acid SRCR domain, this class of proteins have widespread functions as antimicrobial molecules, scavenger receptors, and signalling receptors. Despite the high level of structural conservation of SRCR domains, no unifying mechanism for ligand interaction has been described. The SRCR protein SALSA, also known as DMBT1/gp340, is a key player in mucosal immunology. Based on detailed structural data of SALSA SRCR domains 1 and 8, we here reveal a novel universal ligand-binding mechanism for SALSA ligands. The binding interface incorporates a dual cation-binding site, which is highly conserved across the SRCR superfamily. Along with the well-described cation dependency on most SRCR domain-ligand interactions, our data suggest that the binding mechanism described for the SALSA SRCR domains is applicable to all SRCR domains. We thus propose to have identified in SALSA a conserved functional mechanism for the SRCR class of proteins.
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