University of Worcester Worcester Research and Publications
 
  USER PANEL:
  ABOUT THE COLLECTION:
  CONTACT DETAILS:

Insights into Egg Coat Assembly and Egg-sperm Interaction From the X-ray Structure of Full-length ZP3.

Han, L. and Monné, M. and Okumura, H. and Schwend, T. and Cherry, Amy and Flot, D. and Matsuda, T. and Jovine, L. (2010) Insights into Egg Coat Assembly and Egg-sperm Interaction From the X-ray Structure of Full-length ZP3. Cell, 143 (3). pp. 404-415. ISSN 0092-8674 ESSN: 1097-4172)

[img] Text
1-s2.0-S009286741001127X-main.pdf - Published Version
Restricted to Repository staff only

Download (2MB)

Abstract

ZP3, a major component of the zona pellucida (ZP) matrix coating mammalian eggs, is essential for fertilization by acting as sperm receptor. By retaining a propeptide that contains a polymerization-blocking external hydrophobic patch (EHP), we determined the crystal structure of an avian homolog of ZP3 at 2.0 Å resolution. The structure unveils the fold of a complete ZP domain module in a homodimeric arrangement required for secretion and reveals how EHP prevents premature incorporation of ZP3 into the ZP. This suggests mechanisms underlying polymerization and how local structural differences, reflected by alternative disulfide patterns, control the specificity of ZP subunit interaction. Close relative positioning of a conserved O-glycan important for sperm binding and the hypervariable, positively selected C-terminal region of ZP3 suggests a concerted role in the regulation of species-restricted gamete recognition. Alternative conformations of the area around the O-glycan indicate how sperm binding could trigger downstream events via intramolecular signaling.

Item Type: Article
Additional Information:

Staff and students at the University of Worcester can access the full-text via the Official URL. External users should check availability with their local library or Interlibrary Requests Service.

Uncontrolled Keywords: cell biology, human disease
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Academic Departments > Institute of Science and the Environment
Depositing User: Amy Cherry
Date Deposited: 30 Sep 2013 16:58
Last Modified: 06 Aug 2015 13:26
URI: https://eprints.worc.ac.uk/id/eprint/2416

Actions (login required)

View Item View Item
 
     
Worcester Research and Publications is powered by EPrints 3 which is developed by the School of Electronics and Computer Science at the University of Southampton. More information and software credits.