7C3K
Crystal Structure of mIRGB10
Summary for 7C3K
| Entry DOI | 10.2210/pdb7c3k/pdb |
| Descriptor | Immunity-related GTPase family member b10, GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | mirgb, immune system |
| Biological source | Mus musculus molossinus (Japanese house mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 94296.75 |
| Authors | Ha, H.J.,Jeong, J.H.,Kim, Y.G.,Park, H.H. (deposition date: 2020-05-12, release date: 2021-04-21, Last modification date: 2023-11-29) |
| Primary citation | Ha, H.J.,Chun, H.L.,Lee, S.Y.,Jeong, J.H.,Kim, Y.G.,Park, H.H. Molecular basis of IRGB10 oligomerization and membrane association for pathogen membrane disruption. Commun Biol, 4:92-92, 2021 Cited by PubMed Abstract: Immunity-related GTPase B10 (IRGB10) belongs to the interferon (IFN)-inducible GTPases, a family of proteins critical to host defense. It is induced by IFNs after pathogen infection, and plays a role in liberating pathogenic ligands for the activation of the inflammasome by directly disrupting the pathogen membrane. Although IRGB10 has been intensively studied owing to its functional importance in the cell-autonomous immune response, the molecular mechanism of IRGB10-mediated microbial membrane disruption is still unclear. In this study, we report the structure of mouse IRGB10. Our structural study showed that IRGB10 bound to GDP forms an inactive head-to-head dimer. Further structural analysis and comparisons indicated that IRGB10 might change its conformation to activate its membrane-binding and disruptive functions. Based on this observation, we propose a model of the working mechanism of IRGB10 during pathogen membrane disruption. PubMed: 33469160DOI: 10.1038/s42003-020-01640-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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