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| Title | Cryo-EM structure of pentameric C-reactive protein in complex with monoclonal IgG antibodies. |
|---|---|
| Journal, issue, pages | FEBS J, Year 2025 |
| Publish date | Oct 29, 2025 |
Authors | Andrey V Moiseenko / Alexander V Kalikin / Philipp S Orekhov / Nadezhda A Byzova / Anatoly V Zherdev / Konstantin V Shaitan / Boris B Dzantiev / Olga S Sokolova / ![]() |
| PubMed Abstract | C-reactive protein (CRP) plays a central role in innate immunity and serves as a key biomarker of inflammation. Despite its clinical importance, the structural basis of CRP interactions with ...C-reactive protein (CRP) plays a central role in innate immunity and serves as a key biomarker of inflammation. Despite its clinical importance, the structural basis of CRP interactions with antibodies remains poorly characterized. Using cryo-electron microscopy (cryo-EM), we resolved the structure of immune complexes formed between pentameric CRP and monoclonal immunoglobulin G (IgG) antibodies at up to 2.4 Å resolution. The complexes display a barrel-shaped architecture, with two CRP pentamers bridged by three to five antibodies. We built an atomic model of the CRP-antibody interface, identifying a binding site on the A-face of CRP mediated exclusively by hydrogen bonds, without salt-bridge formation. These findings provide structural insights into CRP-IgG recognition and offer a basis for the rational design of improved antibodies. |
External links | FEBS J / PubMed:41159871 |
| Methods | EM (single particle) |
| Resolution | 2.4 Å |
| Structure data | EMDB-64950, PDB-9vca: |
| Source |
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Keywords | IMMUNE SYSTEM / c-reactive protein / CRP / monoclonal antibody / immune complex / IgG |
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