Biology:Zona pellucida-like domain

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Zona pellucida-like domain
Identifiers
SymbolZona_pellucida
PfamPF00100
InterProIPR001507
SMARTSM00241
PROSITEPDOC00577
Membranome146

The zona pellucida-like domain (ZP domain / ZP-like domain / ZP module)[1][2] is a large protein region of about 260 amino acids. It has been recognised in a variety of receptor-like eukaryotic glycoproteins.[1] All of these molecules are mosaic proteins with a large extracellular region composed of various domains, often followed by either a transmembrane domain and a short cytoplasmic region or by a GPI-anchor.[2]

Functional and crystallographic studies revealed that the "ZP domain" region common to all these proteins is a protein polymerization module that consists of two distinct but structurally related immunoglobulin-like domains, ZP-N and ZP-C, separated by an interdomain linker (ITD).[3][4][5][6][7][8][9] The ZP module is located in the C-terminal portion of the extracellular region and – with the exception of non-polymeric family member ENG[10] – contains 8 or 10 conserved Cys residues involved in disulfide bonds.[4][5][8] The ZP-C domain contains a EHP/IHP motif that controls polymerization.[11]

The first 3D structure of a homopolymeric ZP module protein filament, native human uromodulin (UMOD), was determined by cryo-EM.[12][13]

Additional copies of isolated ZP-N domains are found in the N-terminal region of egg coat protein subunits involved in fertilization in both vertebrates and invertebrates, with the human zona pellucida components ZP1, ZP2 and ZP4 being the best understood.[4][14] The mollusc "vitelline envelope receptor for egg lysin" (VERL, Q8WR62) is found in the vitelline envelope of mollusc eggs and consists of 22 VERL repeats followed by a ZP module. Structural work from 2017 demonstrated that VERL repeats are also ZP-N domains.[15]

Examples

  • CUZD1
  • DMBT1
  • ENG
  • GP2
  • OIT3
  • POMZP3
  • TECTA, TECTB, TGFBR3
  • UMOD, UMODL1
  • ZP1, ZP2, ZP3, ZP4, ZPLD1

References

  1. ↑ 1.0 1.1 "A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor". FEBS Lett. 300 (3): 237–40. 1992. doi:10.1016/0014-5793(92)80853-9. PMID 1313375. Bibcode: 1992FEBSL.300..237B. 
  2. ↑ 2.0 2.1 "Zona pellucida domain proteins". Annu. Rev. Biochem. 74: 83–114. 2005. doi:10.1146/annurev.biochem.74.082803.133039. PMID 15952882. 
  3. ↑ "The ZP domain is a conserved module for polymerization of extracellular proteins". Nat. Cell Biol. 4 (6): 457–61. 2002. doi:10.1038/ncb802. PMID 12021773. 
  4. ↑ 4.0 4.1 4.2 "Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats". Nature 456 (7222): 653–7. 2008. doi:10.1038/nature07599. PMID 19052627. Bibcode: 2008Natur.456..653M.  PDB: 3D4C, 3D4G, 3EF7​
  5. ↑ 5.0 5.1 "Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3". Cell 143 (3): 404–15. 2010. doi:10.1016/j.cell.2010.09.041. PMID 20970175.  PDB: 3NK3, 3NK4​
  6. ↑ "Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-beta binding". Proc Natl Acad Sci U S A 108 (13): 5232–6. 2011. doi:10.1073/pnas.1010689108. PMID 21402931. Bibcode: 2011PNAS..108.5232L.  PDB: 3QW9​
  7. ↑ "Identification of a Novel TGF-β-Binding Site in the Zona Pellucida C-terminal (ZP-C) Domain of TGF-β-Receptor-3 (TGFR-3)". PLOS ONE 8 (6). 2013. doi:10.1371/journal.pone.0067214. PMID 23826237. Bibcode: 2013PLoSO...867214D.  PDB: 4AJV​
  8. ↑ 8.0 8.1 "A structured interdomain linker directs self-polymerization of human uromodulin". Proc. Natl. Acad. Sci. U.S.A. 113 (6): 1552–1557. 2016. doi:10.1073/pnas.1519803113. PMID 26811476. Bibcode: 2016PNAS..113.1552B.  PDB: 4WRN, 5BUP​
  9. ↑ "Structure of Zona Pellucida Module Proteins". Curr. Top. Dev. Biol.. Current Topics in Developmental Biology 130: 413–442. 2018. doi:10.1016/bs.ctdb.2018.02.007. ISBN 978-0-12-809802-8. PMID 29853186. 
  10. ↑ "Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1". Cell Reports 19 (9): 1917–1928. 2017. doi:10.1016/j.celrep.2017.05.011. PMID 28564608.  PDB: 5HZV​
  11. ↑ "A duplicated motif controls assembly of zona pellucida domain proteins". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5922–7. 2004. doi:10.1073/pnas.0401600101. PMID 15079052. Bibcode: 2004PNAS..101.5922J. 
  12. ↑ "Cryo-EM structure of native human uromodulin, a zona pellucida module polymer". EMBO J. 39 (24). 2020. doi:10.15252/embj.2020106807. PMID 33196145.  PDB: 6TQK, 6TQL​
  13. ↑ "Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH". Nat. Struct. Mol. Biol. 29 (3): 190–193. 2022. doi:10.1038/s41594-022-00729-3. PMID 35273390.  PDB: 7PFP, 7Q3N​
  14. ↑ "Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteins.". Bioinformatics 23 (15): 1871–1874. 2007. doi:10.1093/bioinformatics/btm265. PMID 17510169. 
  15. ↑ "Structural Basis of Egg Coat-Sperm Recognition at Fertilization". Cell 169 (7): 1315–1326. 2017. doi:10.1016/j.cell.2017.05.033. PMID 28622512.  PDB: 5II4, 5II5, 5II6, 5MR2, 5IIC, 5IIA, 5IIB, 5MR3​
This article incorporates text from the public domain Pfam and InterPro: IPR001507




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