Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats

Magnus Monné, Ling Han, Thomas Schwend, Sofia Burendahl and Luca Jovine ()
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Magnus Monné: Karolinska Institutet, Hälsovägen 7, SE-141 57 Huddinge, Sweden
Ling Han: Karolinska Institutet, Hälsovägen 7, SE-141 57 Huddinge, Sweden
Thomas Schwend: Karolinska Institutet, Hälsovägen 7, SE-141 57 Huddinge, Sweden
Sofia Burendahl: Karolinska Institutet, Hälsovägen 7, SE-141 57 Huddinge, Sweden
Luca Jovine: Karolinska Institutet, Hälsovägen 7, SE-141 57 Huddinge, Sweden

Nature, 2008, vol. 456, issue 7222, 653-657

Abstract: Fertilization: the first step The first step in mammalian fertilization, where both species specificity and the one-sperm-per-egg norm are enforced, is recognition between coat proteins in the membrane around the egg (the zona pellucida) and sperm. The mouse zona pellucida protein ZP3 is the primary receptor for sperm and its most conserved domain (ZP-N) is also found in many different extracellular proteins with a wide range of biological functions. The crystal structure of the ZP-N domain of ZP3 has now been determined. ZP-N adopts an immunoglobulin-like fold but shares little similarity with other immunoglobulin-like domains, marking it out as a new subtype of this superfamily. As well as providing a glimpse of mammalian fertilization at atomic resolution, the structure of ZP3 ZP-N is of relevance for reproductive medicine and also for diseases such as non-syndromic deafness or renal and vascular disorders, where ZP-N containing proteins are involved.

Date: 2008
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DOI: 10.1038/nature07599

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