scholarly journals Insights into the molecular basis of sperm–egg recognition in mammals

Reproduction ◽  
2004 ◽  
Vol 127 (4) ◽  
pp. 417-422 ◽  
Author(s):  
Tanya Hoodbhoy ◽  
Jurrien Dean
Keyword(s):  
Zona Pellucida ◽  
Three Dimensional ◽  
Explanatory Models ◽  
Dimensional Structure ◽  
Side Chain ◽  
Egg Recognition ◽  
Three Dimensional Structure ◽  
Sperm Binding ◽  
Single Protein

The zona pellucida surrounding the egg and pre-implantation embryo is required for in vivo fertility and early development. Explanatory models of sperm–egg recognition need to take into account the ability of sperm to bind to ovulated eggs, but not to two-cell embryos. For the last two decades, investigators have sought to identify an individual protein or carbohydrate side chain as the ‘sperm receptor’. However, recent genetic data in mice are more consistent with the three-dimensional structure of the zona pellucida, rather than a single protein (or carbohydrate), determining sperm binding. The mouse and human zonae pellucidae contain three glycoproteins (ZP1, ZP2, ZP3) and, following fertilization, ZP2 is proteolytically cleaved. The replacement of endogenous mouse proteins with human ZP2, ZP3 or both does not alter taxon specificity of sperm binding or prevent fertility. Surprisingly, human ZP2 is not cleaved following fertilization and intact ZP2 correlates with persistent sperm binding to two-cell embryos. Taken together, these data support a model in which the cleavage status of ZP2 modulates the three-dimensional structure of the zona pellucida and determines whether sperm bind (uncleaved) or do not (cleaved).

Zona Pellucida Proteins, Fibrils, and Matrix

2020 ◽  
Vol 89 (1) ◽  
pp. 695-715
Author(s):  
Eveline S. Litscher ◽  
Paul M. Wassarman
Keyword(s):  
Extracellular Matrix ◽  
Zona Pellucida ◽  
Three Dimensional ◽  
Structural Features ◽  
Biological Properties ◽  
Preimplantation Development ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Early Embryos ◽  
N Terminus

The zona pellucida (ZP) is an extracellular matrix that surrounds all mammalian oocytes, eggs, and early embryos and plays vital roles during oogenesis, fertilization, and preimplantation development. The ZP is composed of three or four glycosylated proteins, ZP1–4, that are synthesized, processed, secreted, and assembled into long, cross-linked fibrils by growing oocytes. ZP proteins have an immunoglobulin-like three-dimensional structure and a ZP domain that consists of two subdomains, ZP-N and ZP-C, with ZP-N of ZP2 and ZP3 required for fibril assembly. A ZP2–ZP3 dimer is located periodically along ZP fibrils that are cross-linked by ZP1, a protein with a proline-rich N terminus. Fibrils in the inner and outer regions of the ZP are oriented perpendicular and parallel to the oolemma, respectively, giving the ZP a multilayered appearance. Upon fertilization of eggs, modification of ZP2 and ZP3 results in changes in the ZP's physical and biological properties that have important consequences. Certain structural features of ZP proteins suggest that they may be amyloid-like proteins.

The three-dimensional structure of the zona pellucida in growing and atretic ovarian follicles of the mouse

1989 ◽  
Vol 257 (2) ◽  
pp. 247-253 ◽  
Author(s):  
Giuseppe Familiari ◽  
Stefania A. Nottola ◽  
Antonio Familiari ◽  
Pietro M. Motta
Keyword(s):  
Zona Pellucida ◽  
Three Dimensional ◽  
Ovarian Follicles ◽  
Dimensional Structure ◽  
Three Dimensional Structure

scholarly journals Modeling Metabolic Diseases with Organoids: A Review

2021 ◽  
Vol 2 (4) ◽  
pp. 272-279
Author(s):  
JF Bustos ◽  
JC Alvarado Gonzalez ◽  
DAR de Abreu ◽  
H Liebisch-Rey ◽  
A Silva ◽  
...  
Keyword(s):  
Metabolic Diseases ◽  
Functional Unit ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Biological Structure ◽  
Three Dimensional Structure

An organoid is a functional unit of any given organ capable of reproducing under culture, as well as a biological structure similar in both function and structure to its in vivo equivalent. They are miniature-sized functional versions of organs, formed by masses of cells which self-organize to form a three-dimensional structure.

Three-dimensional structure of the zona pellucida at ovulation

2006 ◽  
Vol 69 (6) ◽  
pp. 415-426 ◽  
Author(s):  
Giuseppe Familiari ◽  
Michela Relucenti ◽  
Rosemarie Heyn ◽  
Giulietta Micara ◽  
Silvia Correr
Keyword(s):  
Zona Pellucida ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

NMR three-dimensional structure of the cationic peptide Stigmurin from Tityus stigmurus scorpion venom: In vitro antioxidant and in vivo antibacterial and healing activity

Peptides ◽  
2021 ◽  
Vol 137 ◽  
pp. 170478
Author(s):  
Alessandra Daniele-Silva ◽  
Suedson de Carvalho Silva Rodrigues ◽  
Elizabeth Cristina Gomes dos Santos ◽  
Moacir Fernandes de Queiroz Neto ◽  
Hugo Alexandre de Oliveira Rocha ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Scorpion Venom ◽  
Dimensional Structure ◽  
Cationic Peptide ◽  
Three Dimensional Structure

scholarly journals Crystal structure of ethyl 2-({[(4Z)-3,5-dioxo-1-phenylpyrazolidin-4-ylidene]methyl}amino)acetate

2014 ◽  
Vol 70 (9) ◽  
pp. o938-o939
Author(s):  
Shaaban K. Mohamed ◽  
Mehmet Akkurt ◽  
Joel T. Mague ◽  
Eman A. Ahmed ◽  
Mustafa R. Albayati
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Dihedral Angle ◽  
Title Compound ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Side Chain ◽  
Three Dimensional Structure ◽  
Compound C ◽  
The Mean

The title compound, C14H15N3O4, is nearly planar, the dihedral angle between the planes of the phenyl and pyrazolidine rings being 1.13 (7) Å, and that between the plane of the pyrazolidine ring and the mean plane of the side chain [C—N—C–C(=O)—O; r.m.s. deviation = 0.024 Å] being 2.52 (7)°. This is due in large part to the presence of the intramolecular N—H...O and C—H...O hydrogen bonds. In the crystal, pairwise N—H...O hydrogen bonds form inversion dimers, which are further associated into layers, lying very close to plane (-120),viapairwise C—H...O hydrogen bonds. The layers are then weakly connected through C—H...O hydrogen bonds, forming a three-dimensional structure.

scholarly journals In Vivo and In Vitro Studies of Bacillus subtilis Ferrochelatase Mutants Suggest Substrate Channeling in the Heme Biosynthesis Pathway

2002 ◽  
Vol 184 (14) ◽  
pp. 4018-4024 ◽  
Author(s):  
Ulf Olsson ◽  
Annika Billberg ◽  
Sara Sjövall ◽  
Salam Al-Karadaghi ◽  
Mats Hansson
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Three Dimensional ◽  
Site Directed Mutagenesis ◽  
Dimensional Structure ◽  
Amino Acid Residues ◽  
Three Dimensional Structure ◽  
Activity Measurements

ABSTRACT Ferrochelatase (EC 4.99.1.1) catalyzes the last reaction in the heme biosynthetic pathway. The enzyme was studied in the bacterium Bacillus subtilis, for which the ferrochelatase three-dimensional structure is known. Two conserved amino acid residues, S54 and Q63, were changed to alanine by site-directed mutagenesis in order to detect any function they might have. The effects of these changes were studied in vivo and in vitro. S54 and Q63 are both located at helix α3. The functional group of S54 points out from the enzyme, while Q63 is located in the interior of the structure. None of these residues interact with any other amino acid residues in the ferrochelatase and their function is not understood from the three-dimensional structure. The exchange S54A, but not Q63A, reduced the growth rate of B. subtilis and resulted in the accumulation of coproporphyrin III in the growth medium. This was in contrast to the in vitro activity measurements with the purified enzymes. The ferrochelatase with the exchange S54A was as active as wild-type ferrochelatase, whereas the exchange Q63A caused a 16-fold reduction in V max. The function of Q63 remains unclear, but it is suggested that S54 is involved in substrate reception or delivery of the enzymatic product.

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