5JKD

Crystal structure of human IZUMO1-JUNO complex (crystal form 2)

5JKD の概要

• エントリーDOI: 10.2210/pdb5jkd/pdb
• 関連するPDBエントリー: 5JK9 5JKA 5JKB 5JKC 5JKE
• 分子名称: Izumo sperm-egg fusion protein 1, Sperm-egg fusion protein Juno, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: fertilization, izumo1, juno, cell adhesion
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54070.04

構造登録者

Ohto, U.,Ishida, H.,Shimizu, T. (登録日: 2016-04-26, 公開日: 2016-06-22, 最終更新日: 2024-11-13)

主引用文献

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

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: 27309808
DOI: 10.1038/nature18596

実験手法

X-RAY DIFFRACTION (2.9 Å)