Summary for 6H03
| Entry DOI | 10.2210/pdb6h03/pdb |
| Related | 6H04 |
| EMDB information | 0106 0107 0109 0110 0111 0112 0113 |
| Descriptor | Complement C5,Complement C5, 2-acetamido-2-deoxy-beta-D-glucopyranose, Complement component C8 beta chain, ... (10 entities in total) |
| Functional Keywords | c5b9, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 24 |
| Total formula weight | 1631064.09 |
| Authors | Menny, A.,Serna, M.,Boyd, C.M.,Gardner, S.,Joseph, A.P.,Topf, M.,Bubeck, D. (deposition date: 2018-07-06, release date: 2018-12-19, Last modification date: 2020-07-29) |
| Primary citation | Menny, A.,Serna, M.,Boyd, C.M.,Gardner, S.,Joseph, A.P.,Morgan, B.P.,Topf, M.,Brooks, N.J.,Bubeck, D. CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers. Nat Commun, 9:5316-5316, 2018 Cited by PubMed Abstract: The membrane attack complex (MAC) is one of the immune system's first responders. Complement proteins assemble on target membranes to form pores that lyse pathogens and impact tissue homeostasis of self-cells. How MAC disrupts the membrane barrier remains unclear. Here we use electron cryo-microscopy and flicker spectroscopy to show that MAC interacts with lipid bilayers in two distinct ways. Whereas C6 and C7 associate with the outer leaflet and reduce the energy for membrane bending, C8 and C9 traverse the bilayer increasing membrane rigidity. CryoEM reconstructions reveal plasticity of the MAC pore and demonstrate how C5b6 acts as a platform, directing assembly of a giant β-barrel whose structure is supported by a glycan scaffold. Our work provides a structural basis for understanding how β-pore forming proteins breach the membrane and reveals a mechanism for how MAC kills pathogens and regulates cell functions. PubMed: 30552328DOI: 10.1038/s41467-018-07653-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.6 Å) |
Structure validation
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