By Eveline S. Litscher, Paul M. Wassarman
This ebook presents a coherent, transparent, and uniform presentation of structural, genetic, molecular, and biochemical info to be had for the zona pellucida area protein relatives, which impression pathologies resembling infertility, deafness, and melanoma. additionally it:
- Details information regarding the constitution and serve as of the ZP area in ZPDC-proteins
- Provides illustrations of the association of ZPDC-proteins, the genes that encode the proteins, and examples of mutations within the ZP area that reason diseases
- Speculates as to the evolution of the ZP area and capability therapeutics for ailments stemming from ZP area mutations
- Addresses mammalian and non-mammalian systems
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Extra resources for A Guide to Zona Pellucida Domain Proteins
Further Reading Bleil JD, Wassarman PM. Structure and function of the zona pellucida: identification and characterization of the proteins of the mouse oocyte’s zona pellucida. Dev Biol 76, 185–202 (1980). Boja ES, Hoodbhoy T, Fales HM, Dean J. Structural characterization of native mouse zona pellucida proteins using mass spectrometry. J Biol Chem 278, 34189–34202 (2003). Bork P. A trefoil domain in the major rabbit zona pellucida protein. Protein Sci 2, 669–670 (1993). Callebaut I, Mornon JP, Monget P.
Roller RJ, Wassarman PM. Role of asparagine‐linked oligosaccharides in secretion of glycoproteins of the mouse egg’s extracellular coat. J Biol Chem 258, 13243–13249 (1983). Salzmann GS, Greve JM, Roller RJ, Wassarman PM. Biosynthesis of the sperm receptor during oogenesis in the mouse. EMBO J 2, 1451–1456 (1983). Shimizu S, Tsuji M, Dean J. In vitro biosynthesis of three sulfated glycoproteins of murine zonae pellucidae by oocytes grown in follicle culture. J Biol Chem 258, 5858–5863 (1983).
Jovine L, Janssen WG, Litscher ES, Wassarman PM. The PLAC‐1 homology region of the ZP domain is sufficient for protein polymerization. BMC Biochem 7, 11–19 (2006). Monné M, Han L, Schwend T, Burendahl S, Jovine L. Crystal structure of the ZP‐N domain of ZP3 reveals the core fold of animal egg coats. Nature 456, 653–657 (2008). Monné M, Jovine L. A structural view of egg coat architecture and function in fertilization. Biol Reprod 85, 661–669 (2011). 1; Parts B, C, and D). Protein domains like the ZPD are evolutionary units that can be duplicated and recombined.
A Guide to Zona Pellucida Domain Proteins by Eveline S. Litscher, Paul M. Wassarman