3D4C

ZP-N domain of mammalian sperm receptor ZP3 (crystal form I)

3D4C の概要

• エントリーDOI: 10.2210/pdb3d4c/pdb
• 関連するPDBエントリー: 3D4G 3EF7 3NK3 3NK4
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CADMIUM ION (3 entities in total)
• 機能のキーワード: fertilization, oocyte, egg coat, zona pellucida, vitelline envelope, zp domain, egg-sperm interaction, species-specific gamete recognition, speciation, biodiversity, infertility, extracellular matrix, immunoglobulin-like fold, glycoprotein, receptor, secreted, transmembrane, cell adhesion
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54078.12

構造登録者

Jovine, L.,Monne, M. (登録日: 2008-05-14, 公開日: 2008-12-02, 最終更新日: 2024-10-30)

主引用文献

Monne, M.,Han, L.,Schwend, T.,Burendahl, S.,Jovine, L.
Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats
Nature, 456:653-657, 2008

PubMed Abstract: Species-specific recognition between the egg extracellular matrix (zona pellucida) and sperm is the first, crucial step of mammalian fertilization. Zona pellucida filament components ZP3 and ZP2 act as sperm receptors, and mice lacking either of the corresponding genes produce oocytes without a zona pellucida and are completely infertile. Like their counterparts in the vitelline envelope of non-mammalian eggs and many other secreted eukaryotic proteins, zona pellucida subunits polymerize using a 'zona pellucida (ZP) domain' module, whose conserved amino-terminal part (ZP-N) was suggested to constitute a domain of its own. No atomic structure has been reported for ZP domain proteins, and there is no structural information on any conserved vertebrate protein that is essential for fertilization and directly involved in egg-sperm binding. Here we describe the 2.3 ångström (A) resolution structure of the ZP-N fragment of mouse primary sperm receptor ZP3. The ZP-N fold defines a new immunoglobulin superfamily subtype with a beta-sheet extension characterized by an E' strand and an invariant tyrosine residue implicated in polymerization. The structure strongly supports the presence of ZP-N repeats within the N-terminal region of ZP2 and other vertebrate zona pellucida/vitelline envelope proteins, with implications for overall egg coat architecture, the post-fertilization block to polyspermy and speciation. Moreover, it provides an important framework for understanding human diseases caused by mutations in ZP domain proteins and developing new methods of non-hormonal contraception.

PubMed: 19052627
DOI: 10.1038/nature07599

実験手法

X-RAY DIFFRACTION (2.9 Å)