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PDBsum entry 5jk9

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Top Page protein ligands Protein-protein interface(s) links
Cell adhesion PDB id
5jk9
Contents
Protein chains
241 a.a.
212 a.a.
Ligands
NAG ×6
Waters ×537

References listed in PDB file
Key reference
Title Structure of izumo1-Juno reveals sperm-Oocyte recognition during mammalian fertilization.
Authors U.Ohto, H.Ishida, E.Krayukhina, S.Uchiyama, N.Inoue, T.Shimizu.
Ref. Nature, 2016, 534, 566-569. [DOI no: 10.1038/nature18596]
PubMed id 27309808
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.
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 Headers

 

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