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Eveline S. Litscher, Paul M. Wassarman's A Guide to Zona Pellucida Domain Proteins PDF

By Eveline S. Litscher, Paul M. Wassarman

ISBN-10: 0470528117

ISBN-13: 9780470528112

ISBN-10: 1119044723

ISBN-13: 9781119044727

ISBN-10: 1119044766

ISBN-13: 9781119044765

ISBN-10: 1119044995

ISBN-13: 9781119044994

This publication offers a coherent, transparent, and uniform presentation of structural, genetic, molecular, and biochemical details on hand for the zona pellucida area protein kin, which influence pathologies similar to infertility, deafness, and melanoma. moreover 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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Additional resources for A Guide to Zona Pellucida Domain Proteins

Sample text

PLoS One 8, 9 (2013). Qi H, Williams Z, Wassarman PM. Secretion and assembly of zona pellucida glycoproteins by growing mouse oocytes microinjected with epitope‐tagged cDNAs for mZP2 and mZP3. Mol Cell Biol 13, 530–541 (2002). 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.

Proteins only occurs shortly before or just after the release of nascent mZP1–3 into the extracellular space. Nascent mZP2 and 3 are associated only with the innermost region of the thickening ZP, proximal to the oocyte’s plasma membrane. 1). An mZP2–mZP3 dimer is located every ≃14 nm or so along the fibrils, imposing a structural periodicity that can be visualized in electron micrographs of solubilized mouse ZP. The fibrils in turn are crosslinked by mZP1, the least abundant of the ZP proteins, to create a 3‐dimensional matrix.

437 aa). 3 Chicken ZP3 homodimer structure formed by two ZP modules each consisting of a ZP‐N and ZP‐C sub‐domain. Dashed lines represent disordered loops. Reproduced with permission from Han et al. (2010). © Elsevier. For color detail, please see color plate section. ] The protein was expressed in Chinese hamster ovary cells and secreted as an ≃80 kD MW soluble homodimer. 4 Topology scheme of chicken ZP3 with secondary structure and disulfide connectivity. Reproduced with permission from Han et al.

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A Guide to Zona Pellucida Domain Proteins by Eveline S. Litscher, Paul M. Wassarman

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