ZP DOMAIN STRUCTURE · Structure determination of the zona pellucida domain by X-ray crystallography
FP6 — Marie Curie Actions (Human Resources and Mobility)
- Duration
- 2006-04-01 → 2007-03-31
- EU contribution
- €40,000
- Participants
- 1
- Scheme
- ERG
Lines connect the coordinator with its partners.
Results in brief
Final Activity Report Summary - ZP DOMAIN STRUCTURE (Structure determination of the zona pellucida domain by X-ray crystallography)
Fertilisation is a fundamental process necessary for the continuation of mankind and other species. Surprisingly little is known about it on the molecular level. The aim of this project has been to try to understand how the zona pellucida (ZP) coat that surrounds the egg works. The ZP is build up by long filaments of glycoprotein subunits that form a three-dimensional network around the egg. ZP proteins participate in the species-specific recognition of sperm and in blocking more sperms from binding to the egg after the first gamete fusion event. All contain a so-called ZP domain that is responsible for their polymerisation into filaments. We have determined the spatial organisation of the atoms making up the most conserved part of this domain. The results improve our knowledge of fertilisation in general and are crucial for explaining mutations in human ZP domain proteins that cause disease.
Data: CORDIS, © European Union
Project objective
For all sexually reproducing organisms fertilisation is a fundamental step to ensure the continuity of the species. The events that take place during fertilisation are poorly understood at the molecular level, although a number of components that play crucial roles in this process have been identified in mammals. The mammalian oocyte is surrounded by the zona pellucida (ZP), a specialised extra-cellular matrix consisting of filaments of polymerised ZP domain proteins. Some of these ZP domain proteins serve a s species-specific receptors for the initial recognition of sperm. Upon fusion of the gametes, modification of ZP subunits leads to morphological changes of the whole matrix that inactivate its receptor activity as part of the block against the entry of additional sperm.The goal of this project is to determine the first three-dimensional structure of a ZP domain. So far, no structure is available for this conserved protein, which is thought to adopt a unique fold. Solving the structure would be of outmost importance for understanding the molecular mechanism of crucial steps of fertilisation. Since more than one hundred extra-cellular proteins with diverse functions contain ZP domains, a structure would have implications far beyond the field of fertilisation and it would allow detailed interpretation of the effect of the many ZP domain mutations that cause disease in humans.
Original text from CORDIS.
Participants
- KAROLINSKA INSTITUTET · STOCKHOLMCoordinatorSweden
Links
Data: CORDIS, © European Union