3NK3
Crystal structure of full-length sperm receptor ZP3 at 2.6 A resolution
Summary for 3NK3
| Entry DOI | 10.2210/pdb3nk3/pdb |
| Related | 3D4C 3D4G 3EF7 3NK4 |
| Related PRD ID | PRD_900084 |
| Descriptor | Zona pellucida 3, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose, CITRATE ANION, ... (5 entities in total) |
| Functional Keywords | fertilization, oocyte, egg coat, zona pellucida, vitelline envelope, zp domain, zp module, egg-sperm interaction, species-specific gamete recognition, speciation, biodiversity, infertility, extracellular matrix, immunoglobulin-like fold, glycoprotein, receptor, secreted, transmembrane, cell adhesion, o-linked carbohydrate, t-antigen, core-1, external hydrophobic patch, ehp, internal hydrophobic patch, ihp, sperm-combining site |
| Biological source | Gallus gallus (bantam,chickens) More |
| Total number of polymer chains | 4 |
| Total formula weight | 72178.76 |
| Authors | Monne, M.,Jovine, L. (deposition date: 2010-06-18, release date: 2010-11-10, Last modification date: 2023-09-06) |
| Primary citation | Han, L.,Monne, M.,Okumura, H.,Schwend, T.,Cherry, A.L.,Flot, D.,Matsuda, T.,Jovine, L. Insights into Egg Coat Assembly and Egg-Sperm Interaction from the X-Ray Structure of Full-Length ZP3. Cell(Cambridge,Mass.), 143:404-415, 2010 Cited by PubMed Abstract: ZP3, a major component of the zona pellucida (ZP) matrix coating mammalian eggs, is essential for fertilization by acting as sperm receptor. By retaining a propeptide that contains a polymerization-blocking external hydrophobic patch (EHP), we determined the crystal structure of an avian homolog of ZP3 at 2.0 Å resolution. The structure unveils the fold of a complete ZP domain module in a homodimeric arrangement required for secretion and reveals how EHP prevents premature incorporation of ZP3 into the ZP. This suggests mechanisms underlying polymerization and how local structural differences, reflected by alternative disulfide patterns, control the specificity of ZP subunit interaction. Close relative positioning of a conserved O-glycan important for sperm binding and the hypervariable, positively selected C-terminal region of ZP3 suggests a concerted role in the regulation of species-restricted gamete recognition. Alternative conformations of the area around the O-glycan indicate how sperm binding could trigger downstream events via intramolecular signaling. PubMed: 20970175DOI: 10.1016/j.cell.2010.09.041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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