{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kadava T"],"funding":["Dutch Research Council (NWO)"],"pagination":["101046"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12419116"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(9)"],"pubmed_abstract":["C4b-binding protein (C4BP) is an innate immune inhibitor found in serum. Human C4BP adopts spider-like higher-order structures (HOS) formed by disulfide-linked C4BPα and C4BPβ chains that non-covalently bind vitamin K-dependent protein S (ProS). These spider-like structures can form even larger complexes as C4BP interacts with other, mostly complement-related, proteins. The complement inhibitory role of C4BP is primarily mediated through its interaction with C4b. C4BP also binds with high affinity to serum amyloid P component (SAP), a pentraxin family member associated with amyloidosis conditions. Here, we structurally and compositionally characterize C4BP interactions with these two natively occurring binders. To achieve this, we combine mass photometry, high-speed atomic force microscopy"],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["Structural Insights Into Complement Inhibition: Visualizing Distinct Binding Modes of C4b-Binding Protein Complexes With C4b and SAP."],"pmcid":["PMC12419116"],"funding_grant_id":["SPI.2017.028"],"pubmed_authors":["Strasser J","Heck AJR","Kadava T","Yin VC","Preiner J","Trouw LA","Marefat M"],"additional_accession":[]},"is_claimable":false,"name":"Structural Insights Into Complement Inhibition: Visualizing Distinct Binding Modes of C4b-Binding Protein Complexes With C4b and SAP.","description":"C4b-binding protein (C4BP) is an innate immune inhibitor found in serum. Human C4BP adopts spider-like higher-order structures (HOS) formed by disulfide-linked C4BPα and C4BPβ chains that non-covalently bind vitamin K-dependent protein S (ProS). These spider-like structures can form even larger complexes as C4BP interacts with other, mostly complement-related, proteins. The complement inhibitory role of C4BP is primarily mediated through its interaction with C4b. C4BP also binds with high affinity to serum amyloid P component (SAP), a pentraxin family member associated with amyloidosis conditions. Here, we structurally and compositionally characterize C4BP interactions with these two natively occurring binders. To achieve this, we combine mass photometry, high-speed atomic force microscopy","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-06-02T17:45:44.705Z","creation":"2026-05-27T03:07:42.691Z"},"accession":"S-EPMC12419116","cross_references":{"pubmed":["40754140"],"doi":["10.1016/j.mcpro.2025.101046"]}}