Bioinformatics Advance Access published online on May 17, 2007
Bioinformatics, doi:10.1093/bioinformatics/btm265
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Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteins
1 Département de Biologie Structurale, IMPMC UMR 7590; Universités Pierre et Marie Curie-Paris6 et Denis Diderot-Paris7; CNRS; Campus Boucicaut, 140 rue de Lourmel, 75015 Paris, France.
2 INRA Physiologie de la Reproduction et des Comportements, UMR6175 INRA - CNRS - Université de Tours- Haras Nationaux, 37380 Nouzilly, France.
*To whom correspondence should be addressed. Isabelle Callebaut, E-mail: isabelle.callebaut{at}impmc.jussieu.fr
| Abstract |
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Motivation: Zona Pellucida (ZP) domains have been found in a wide variety of extracellular proteins, in which they play essential role for polymeri-zation. They are shared by the ZP proteins, which constitute the extracellular coat of animal eggs. Except from ZP3, constituting the primary sperm receptor, the ZP proteins possess, in addition to their C-terminal ZP domains, N-terminal extensions, which are thought to play an important role in the species-specific gamete recognition. Here, we show that these extensions are made of single or multiple copies of a small globular domain, which can be significantly related to the N-terminal region of ZP domains (ZP-N domains). This finding brings new insights into the molecular evolution of ZP proteins, which may have evolved around a common ZP-N architecture, and more generally into the noticeable sequence diversity of ZP-N do-mains, which can be found as isolated subunits or tightly associated with ZP-C domains to form complete, canonical ZP domains.
Supplementary information: supplementary data for this article are available at Bioinformatics on line.
Associate Editor: Dr. Alex Bateman
Received on February 12, 2007; revised on May 9, 2007; accepted on May 10, 2007
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