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Zona pellucida-like domain
Identifiers
SymbolZona_pellucida
Pfam PF00100
InterPro IPR001507
SMART SM00241
PROSITE PDOC00577
Membranome 146
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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 region and a very 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. [3] [4] [5] [6] [7] [8] [9] [10] The ZP module is located in the C-terminal portion of the extracellular region and – with the exception of non-polymeric family member ENG [11] – contains 8 or 10 conserved Cys residues involved in disulfide bonds. [5] [6] [9]

The first 3D structure of a 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, such as human zona pellucida components ZP1, ZP2 and ZP4 and mollusk vitelline envelope receptor for egg lysin (VERL). [5] [14] [15]

Examples

Humans genes encoding proteins containing this domain include:

References

  1. ^ a b Bork P, Sander C (1992). "A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor". FEBS Lett. 300 (3): 237–40. doi: 10.1016/0014-5793(92)80853-9. PMID  1313375. S2CID  38778076.
  2. ^ a b Jovine L, Darie CC, Litscher ES, Wassarman PM (2005). "Zona pellucida domain proteins". Annu. Rev. Biochem. 74: 83–114. doi: 10.1146/annurev.biochem.74.082803.133039. PMID  15952882.
  3. ^ Jovine L, Qi H, Williams Z, Litscher E, Wassarman PM (2002). "The ZP domain is a conserved module for polymerization of extracellular proteins". Nat. Cell Biol. 4 (6): 457–61. doi: 10.1038/ncb802. PMID  12021773. S2CID  11575790.
  4. ^ Jovine L, Qi H, Williams Z, Litscher ES, Wassarman PM (2004). "A duplicated motif controls assembly of zona pellucida domain proteins". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5922–7. Bibcode: 2004PNAS..101.5922J. doi: 10.1073/pnas.0401600101. PMC  395899. PMID  15079052.
  5. ^ a b c Monné M, Han L, Schwend T, Burendahl S, Jovine L (2008). "Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats". Nature. 456 (7222): 653–7. Bibcode: 2008Natur.456..653M. doi: 10.1038/nature07599. hdl: 11563/8930. PMID  19052627. S2CID  4430083. PDB: 3D4C, 3D4G, 3EF7​
  6. ^ a b Han L, Monné M, Okumura, H, Schwend, T, Cherry, AL, Flot, D, Matsuda, T, Jovine, L (2010). "Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3". Cell. 143 (3): 404–15. doi: 10.1016/j.cell.2010.09.041. hdl: 11563/8931. PMID  20970175. S2CID  18583237. PDB: 3NK3, 3NK4​
  7. ^ Lin SJ, Hu Y, Zhu J, Woodruff TK, Jardetzky TS (2011). "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. Bibcode: 2011PNAS..108.5232L. doi: 10.1073/pnas.1010689108. PMC  3069177. PMID  21402931. PDB: 3QW9​
  8. ^ Diestel U, Resch M, Meinhardt K, Weiler S, Hellmann TV, Mueller TD, Nickel J, Eichler J, Muller YA (2013). "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): e67214. Bibcode: 2013PLoSO...867214D. doi: 10.1371/journal.pone.0067214. PMC  3695229. PMID  23826237. PDB: 4AJV​
  9. ^ a b Bokhove M, Nishimura K, Brunati M, Han L, de Sanctis D, Rampoldi L, Jovine L (2016). "A structured interdomain linker directs self-polymerization of human uromodulin". Proc. Natl. Acad. Sci. U.S.A. 113 (6): 1552–1557. Bibcode: 2016PNAS..113.1552B. doi: 10.1073/pnas.1519803113. PMC  4760807. PMID  26811476. PDB: 4WRN, 5BUP​
  10. ^ Bokhove M, Jovine L (2018). "Structure of Zona Pellucida Module Proteins". Curr. Top. Dev. Biol. Current Topics in Developmental Biology. 130: 413–442. doi: 10.1016/bs.ctdb.2018.02.007. ISBN  9780128098028. PMID  29853186.
  11. ^ Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L (2017). "Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1". Cell Reports. 19 (9): 1917–1928. doi: 10.1016/j.celrep.2017.05.011. PMC  5464963. PMID  28564608. PDB: 5HZV​
  12. ^ Stsiapanava A, Xu C, Brunati M, Zamora-Caballero S, Schaeffer C, Bokhove M, Han L, Hebert H, Carroni M, Yasumasu S, Rampoldi L, Wu B, Jovine L (2020). "Cryo-EM structure of native human uromodulin, a zona pellucida module polymer". EMBO J. 39 (24): e106807. doi: 10.15252/embj.2020106807. PMC  7737619. PMID  33196145. bioRxiv  10.1101/2020.05.28.119206 PDB: 6TQK, 6TQL​
  13. ^ Stsiapanava A, Xu C, Nishio S, Han L, Yamakawa N, Carroni M, Tunyasuvunakool K, Jumper J, de Sanctis D, Wu B, Jovine L (2022). "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. doi: 10.1038/s41594-022-00729-3. PMC  8930769. PMID  35273390. PDB: 7PFP, 7Q3N​
  14. ^ Callebaut I, Mornon JP, Monget P (2007). "Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteins". Bioinformatics. 23 (15): 1871–1874. doi: 10.1093/bioinformatics/btm265. PMID  17510169.
  15. ^ Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L (2017). "Structural Basis of Egg Coat-Sperm Recognition at Fertilization". Cell. 169 (7): 1315–1326. doi: 10.1016/j.cell.2017.05.033. PMC  5480393. 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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