5F4Q

Crystal structure of the human egg surface protein Juno

5F4Q の概要

• エントリーDOI: 10.2210/pdb5f4q/pdb
• 関連するPDBエントリー: 5F4E 5F4T 5F4V
• 分子名称: Sperm-egg fusion protein Juno, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: glycoprotein, membrane-bound, cysteine-rich, receptor, cell adhesion
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane ; Lipid-anchor, GPI-anchor : A6ND01
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 99606.65

構造登録者

Aydin, H.,Sultana, A.,Lee, J.E. (登録日: 2015-12-03, 公開日: 2016-06-15, 最終更新日: 2024-11-06)

主引用文献

Aydin, H.,Sultana, A.,Li, S.,Thavalingam, A.,Lee, J.E.
Molecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complex.
Nature, 534:562-565, 2016

PubMed Abstract: Fertilization is an essential biological process in sexual reproduction and comprises a series of molecular interactions between the sperm and egg. The fusion of the haploid spermatozoon and oocyte is the culminating event in mammalian fertilization, enabling the creation of a new, genetically distinct diploid organism. The merger of two gametes is achieved through a two-step mechanism in which the sperm protein IZUMO1 on the equatorial segment of the acrosome-reacted sperm recognizes its receptor, JUNO, on the egg surface. This recognition is followed by the fusion of the two plasma membranes. IZUMO1 and JUNO proteins are indispensable for fertilization, as constitutive knockdown of either protein results in mice that are healthy but infertile. Despite their central importance in reproductive medicine, the molecular architectures of these proteins and the details of their functional roles in fertilization are not known. Here we present the crystal structures of human IZUMO1 and JUNO in unbound and bound conformations. The human IZUMO1 structure exhibits a distinct boomerang shape and provides structural insights into the IZUMO family of proteins. Human IZUMO1 forms a high-affinity complex with JUNO and undergoes a major conformational change within its N-terminal domain upon binding to the egg-surface receptor. Our results provide insights into the molecular basis of sperm-egg recognition, cross-species fertilization, and the barrier to polyspermy, thereby promising benefits for the rational development of non-hormonal contraceptives and fertility treatments for humans and other mammals.

PubMed: 27309818
DOI: 10.1038/nature18595

実験手法

X-RAY DIFFRACTION (1.8 Å)