ArticleProceedings of the National Academy of Sciences of the United States of America2020
Missing regions within the molecular architecture of human fibrin clots structurally resolved by XL-MS and integrative structural modeling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 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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19 citing papers in PubMed, 36 citations in OpenAlex.
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- Fibrinogen post-translational modifications are biochemical determinants of fibrin clot properties and interactions.The FEBS journal · 2025Review
- FRET-guided modeling of nucleic acids.Nucleic acids research · 2024Article
- Computational Prediction of the Interaction of Ivermectin with Fibrinogen.International journal of molecular sciences · 2023Article
- Real-Time Library Search Increases Cross-Link Identification Depth across All Levels of Sample Complexity.Analytical chemistry · 2023Article
- Towards a structurally resolved human protein interaction network.Nature structural & molecular biology · 2023Article
- Microscale structural changes of individual fibrin fibers during fibrinolysis.Acta biomaterialia · 2022Article
- Label-free visual proteomics: Coupling MS- and EM-based approaches in structural biology.Molecular cell · 2022Review
- A Crosslinking Mass Spectrometry Protocol for the Structural Analysis of Microtubule-Associated Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Notch-Jagged signaling complex defined by an interaction mosaic.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Anomalous mechanics of ZnProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Proteomic Approaches to Study SARS-CoV-2 Biology and COVID-19 Pathology.Journal of proteome research · 2021Article
- Fibrinogen and Fibrin.Sub-cellular biochemistry · 2021Review
- Type I Collagen-Fibrin Mixed Hydrogels: Preparation, Properties and Biomedical Applications.Gels (Basel, Switzerland) · 2020Review
- A synthetic peptide library for benchmarking crosslinking-mass spectrometry search engines for proteins and protein complexes.Nature communications · 2020Article
- Missing regions within the molecular architecture of human fibrin clots structurally resolved by XL-MS and integrative structural modeling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon activation, fibrinogen forms large fibrin biopolymers that coalesce into clots which assist in wound healing. Limited insights into their molecular architecture, due to the sheer size and the insoluble character of fibrin clots, have restricted our ability to develop novel treatments for clotting diseases. The, so far resolved, disparate structural details have provided insights into linear elongation; however, molecular details like the C-terminal domain of the α-chain, the heparin-binding domain on the β-chain, and other functional domains remain elusive. To illuminate these dark areas, we applied cross-linking mass spectrometry (XL-MS) to obtain biochemical evidence in the form of over 300 distance constraints and combined this with structural modeling. These restraints additionally define the interaction network of the clots and provide molecular details for the interaction with human serum albumin (HSA). We were able to construct the structural models of the fibrinogen α-chain (excluding two highly flexible regions) and the N termini of the β-chain, confirm these models with known structural arrangements, and map how the structure laterally aggregates to form intricate lattices together with the γ-chain. We validate the final model by mapping mutations leading to impaired clot formation. From a list of 22 mutations, we uncovered structural features for all, including a crucial role for βArg'169 (UniProt: 196) in lateral aggregation. The resulting model can potentially serve for research on dysfibrinogenemia and amyloidosis as it provides insights into the molecular mechanisms of thrombosis and bleeding disorders related to fibrinogen variants. The structure is provided in the PDB-DEV repository (PDBDEV_00000030).
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