{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T03:51:06Z","timestamp":1768708266338,"version":"3.49.0"},"reference-count":26,"publisher":"Oxford University Press (OUP)","issue":"15","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2007,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Zona Pellucida (ZP) domains have been found in a wide variety of extracellular proteins, in which they play essential role for polymerization. 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 domains, which can be found as isolated subunits or tightly associated with ZP-C domains to form complete, canonical ZP domains.<\/jats:p><jats:p>Contact: \u00a0isabelle.callebaut@impmc.jussieu.fr<\/jats:p><jats:p>Supplementary information: Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btm265","type":"journal-article","created":{"date-parts":[[2007,5,18]],"date-time":"2007-05-18T16:49:30Z","timestamp":1179506970000},"page":"1871-1874","source":"Crossref","is-referenced-by-count":46,"title":["Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteins"],"prefix":"10.1093","volume":"23","author":[{"given":"Isabelle","family":"Callebaut","sequence":"first","affiliation":[{"name":"1 D\u00e9partement de Biologie Structurale, IMPMC UMR 7590, Universit\u00e9s Pierre et Marie Curie-Paris6 et Denis Diderot-Paris7, CNRS, Campus Boucicaut, 140 rue de Lourmel, 75015 Paris and 2INRA Physiologie de la Reproduction et des Comportements, UMR6175 INRA \u2013 CNRS - Universit\u00e9 de Tours \u2013 Haras Nationaux, 37380 Nouzilly, France"}]},{"given":"Jean-Paul","family":"Mornon","sequence":"additional","affiliation":[{"name":"1 D\u00e9partement de Biologie Structurale, IMPMC UMR 7590, Universit\u00e9s Pierre et Marie Curie-Paris6 et Denis Diderot-Paris7, CNRS, Campus Boucicaut, 140 rue de Lourmel, 75015 Paris and 2INRA Physiologie de la Reproduction et des Comportements, UMR6175 INRA \u2013 CNRS - Universit\u00e9 de Tours \u2013 Haras Nationaux, 37380 Nouzilly, France"}]},{"given":"Philippe","family":"Monget","sequence":"additional","affiliation":[{"name":"1 D\u00e9partement de Biologie Structurale, IMPMC UMR 7590, Universit\u00e9s Pierre et Marie Curie-Paris6 et Denis Diderot-Paris7, CNRS, Campus Boucicaut, 140 rue de Lourmel, 75015 Paris and 2INRA Physiologie de la Reproduction et des Comportements, UMR6175 INRA \u2013 CNRS - Universit\u00e9 de Tours \u2013 Haras Nationaux, 37380 Nouzilly, France"}]}],"member":"286","published-online":{"date-parts":[[2007,5,17]]},"reference":[{"key":"2023041105311242900_","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"2023041105311242900_","doi-asserted-by":"crossref","first-page":"34189","DOI":"10.1074\/jbc.M304026200","article-title":"Structural characterization of native mouse zona pellucida proteins using mass spectrometry","volume":"278","author":"Boja","year":"2003","journal-title":"J. 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