5JKC
Crystal structure of human IZUMO1-JUNO complex (crystal form 1)
Summary for 5JKC
| Entry DOI | 10.2210/pdb5jkc/pdb |
| Related | 5JK9 5JKA 5JKB 5JKD 5JKE |
| Descriptor | Izumo sperm-egg fusion protein 1, Sperm-egg fusion protein Juno, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | fertilization, izumo1, juno, cell adhesion |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 54070.04 |
| Authors | Ohto, U.,Ishida, H.,Shimizu, T. (deposition date: 2016-04-26, release date: 2016-06-22, Last modification date: 2024-10-23) |
| Primary citation | Ohto, U.,Ishida, H.,Krayukhina, E.,Uchiyama, S.,Inoue, N.,Shimizu, T. Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian fertilization Nature, 534:566-569, 2016 Cited by PubMed Abstract: Fertilization is a fundamental process in sexual reproduction, creating a new individual through the combination of male and female gametes. The IZUMO1 sperm membrane protein and its counterpart oocyte receptor JUNO have been identified as essential factors for sperm-oocyte interaction and fusion. However, the mechanism underlying their specific recognition remains poorly defined. Here, we show the crystal structures of human IZUMO1, JUNO and the IZUMO1-JUNO complex, establishing the structural basis for the IZUMO1-JUNO-mediated sperm-oocyte interaction. IZUMO1 exhibits an elongated rod-shaped structure comprised of a helical bundle IZUMO domain and an immunoglobulin-like domain that are each firmly anchored to an intervening β-hairpin region through conserved disulfide bonds. The central β-hairpin region of IZUMO1 provides the main platform for JUNO binding, while the surface located behind the putative JUNO ligand binding pocket is involved in IZUMO1 binding. Structure-based mutagenesis analysis confirms the biological importance of the IZUMO1-JUNO interaction. This structure provides a major step towards elucidating an essential phase of fertilization and it will contribute to the development of new therapeutic interventions for fertility, such as contraceptive agents. PubMed: 27309808DOI: 10.1038/nature18596 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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