ArticleThe Journal of biological chemistry2011
Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 107 citations in OpenAlex.
- Protein Posttranslational Modifications in Immunity: Molecular Mechanisms and Therapeutic Targets.MedComm · 2026Review
- Molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2.Nature communications · 2026Article
- Advances in cryo-EM that have shaped mechanistic models of membrane-attack-complex assembly and regulation.IUCrJ · 2026Review
- From a single C-mannose to multiple C-mannosyltransferases.The Journal of biological chemistry · 2026Review
- Proteolytic profiling of human plasma reveals an immunoactive complement C3 fragment.The EMBO journal · 2025Article
- Action of the Terminal Complement Pathway on Cell Membranes.The Journal of membrane biology · 2025Review
- Quantitative proteomics identifies plasma protein alterations that associate with metabolic and thrombotic profile changes after bariatric surgery.Diabetes, obesity & metabolism · 2025Article
- Review
- Structural basis for membrane attack complex inhibition by CD59.Nature communications · 2023Article
- Towards Understanding the Function of Aegerolysins.Toxins · 2022Review
- Membrane attack complexes, endothelial cell activation, and direct allorecognition.Frontiers in immunology · 2022Review
- Lipid-Binding Aegerolysin from Biocontrol FungusToxins · 2021Article
- Structural basis of soluble membrane attack complex packaging for clearance.Nature communications · 2021Article
- ProteinMolecules (Basel, Switzerland) · 2021Review
- Yeast- and antibody-based tools for studying tryptophan C-mannosylation.Nature chemical biology · 2021Article
- Selective cross-linking of coinciding protein assemblies by in-gel cross-linking mass spectrometry.The EMBO journal · 2021Article
- How Structures of Complement Complexes Guide Therapeutic Design.Sub-cellular biochemistry · 2021Review
- Sequence Diversity in the Pore-Forming Motifs of the Membrane-Damaging Protein Toxins.The Journal of membrane biology · 2020Review
- Article
- Proteomic Analysis of Human Serum from Patients with Chronic Kidney Disease.Biomolecules · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
C8 is one of five complement proteins that assemble on bacterial membranes to form the lethal pore-like "membrane attack complex" (MAC) of complement. The MAC consists of one C5b, C6, C7, and C8 and 12-18 molecules of C9. C8 is composed of three genetically distinct subunits, C8α, C8β, and C8γ. The C6, C7, C8α, C8β, and C9 proteins are homologous and together comprise the MAC family of proteins. All contain N- and C-terminal modules and a central 40-kDa membrane attack complex perforin (MACPF) domain that has a key role in forming the MAC pore. Here, we report the 2.5 Å resolution crystal structure of human C8 purified from blood. This is the first structure of a MAC family member and of a human MACPF-containing protein. The structure shows the modules in C8α and C8β are located on the periphery of C8 and not likely to interact with the target membrane. The C8γ subunit, a member of the lipocalin family of proteins that bind and transport small lipophilic molecules, shows no occupancy of its putative ligand-binding site. C8α and C8β are related by a rotation of ∼22° with only a small translational component along the rotation axis. Evolutionary arguments suggest the geometry of binding between these two subunits is similar to the arrangement of C9 molecules within the MAC pore. This leads to a model of the MAC that explains how C8-C9 and C9-C9 interactions could facilitate refolding and insertion of putative MACPF transmembrane β-hairpins to form a circular pore.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.