6gf7

From Proteopedia

(Difference between revisions)

Current revision

Molecular basis of egg coat filament cross-linking: Zn-SAD structure of the partially deglycosylated ZP1 ZP-N1 domain homodimer

Structural highlights

6gf7 is a 2 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	6gf6, 6gf8
Gene:	ZP1 (CHICK)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Mammalian fertilisation begins when sperm interacts with the egg zona pellucida (ZP), whose ZP1 subunit is important for fertility by covalently cross-linking ZP filaments into a three-dimensional matrix. Like ZP4, a structurally-related component absent in the mouse, ZP1 is predicted to contain an N-terminal ZP-N domain of unknown function. Here we report a characterisation of ZP1 proteins carrying mutations from infertile patients, which suggests that, in human, filament cross-linking by ZP1 is crucial to form a stable ZP. We map the function of ZP1 to its ZP-N1 domain and determine crystal structures of ZP-N1 homodimers from a chicken homolog of ZP1. These reveal that ZP filament cross-linking is highly plastic and can be modulated by ZP1 fucosylation and, potentially, zinc sparks. Moreover, we show that ZP4 ZP-N1 forms non-covalent homodimers in chicken but not in human. Together, these data identify human ZP1 cross-links as a promising target for non-hormonal contraception.

Molecular basis of egg coat cross-linking sheds light on ZP1-associated female infertility.,Nishimura K, Dioguardi E, Nishio S, Villa A, Han L, Matsuda T, Jovine L Nat Commun. 2019 Jul 12;10(1):3086. doi: 10.1038/s41467-019-10931-5. PMID:31300655^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nishimura K, Dioguardi E, Nishio S, Villa A, Han L, Matsuda T, Jovine L. Molecular basis of egg coat cross-linking sheds light on ZP1-associated female infertility. Nat Commun. 2019 Jul 12;10(1):3086. doi: 10.1038/s41467-019-10931-5. PMID:31300655 doi:http://dx.doi.org/10.1038/s41467-019-10931-5

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6gf7"

@@ Line 3: / Line 3: @@
 <StructureSection load='6gf7' size='340' side='right'caption='[[6gf7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6gf7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GF7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6gf7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GF7 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gf6|6gf6]], [[6gf8|6gf8]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gf7 OCA], [http://pdbe.org/6gf7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gf7 RCSB], [http://www.ebi.ac.uk/pdbsum/6gf7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gf7 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-As the result of a combined biochemical and electron microscopic investigation, hitherto unrecognized structural features of the mouse egg extracellular coat, or zona pellucida, have been revealed. Specimens were prepared for electron microscopy by spraying individually isolated zonae pellucidae onto a substrate and were observed by both rotary shadowing and negative staining techniques. Results of these experiments suggest that the three zona pellucida glycoproteins, ZP1 (200,000 Mr), ZP2 (120,000 Mr) and ZP3 (83,000 Mr), are organized into long filaments. Negatively stained zona pellucida filaments resemble "beads-on-a-string", with each bead (9.5 nm in diameter) located every 17 nm or so (center-to-center distance) along the axis of the filament. The filaments, in turn, appear to be interconnected by one of the three zona pellucida glycoproteins, ZP1, giving rise to a three-dimensional matrix. Proteolysis of ZP1 by chymotrypsin or reduction of intermolecular disulfides of ZP1 by dithiothreitol results in both solubilization of zonae pellucidae and disruption of interconnections between individual zona pellucida filaments. These observations suggest that the zona pellucida, which plays important roles both during and after fertilization of mammalian eggs, is a highly organized extracellular coat in which glycoproteins are assembled into filaments possessing a recognizable structural repeat.
+Mammalian fertilisation begins when sperm interacts with the egg zona pellucida (ZP), whose ZP1 subunit is important for fertility by covalently cross-linking ZP filaments into a three-dimensional matrix. Like ZP4, a structurally-related component absent in the mouse, ZP1 is predicted to contain an N-terminal ZP-N domain of unknown function. Here we report a characterisation of ZP1 proteins carrying mutations from infertile patients, which suggests that, in human, filament cross-linking by ZP1 is crucial to form a stable ZP. We map the function of ZP1 to its ZP-N1 domain and determine crystal structures of ZP-N1 homodimers from a chicken homolog of ZP1. These reveal that ZP filament cross-linking is highly plastic and can be modulated by ZP1 fucosylation and, potentially, zinc sparks. Moreover, we show that ZP4 ZP-N1 forms non-covalent homodimers in chicken but not in human. Together, these data identify human ZP1 cross-links as a promising target for non-hormonal contraception.
-Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat.,Greve JM, Wassarman PM J Mol Biol. 1985 Jan 20;181(2):253-64. PMID:3845123<ref>PMID:3845123</ref>
+Molecular basis of egg coat cross-linking sheds light on ZP1-associated female infertility.,Nishimura K, Dioguardi E, Nishio S, Villa A, Han L, Matsuda T, Jovine L Nat Commun. 2019 Jul 12;10(1):3086. doi: 10.1038/s41467-019-10931-5. PMID:31300655<ref>PMID:31300655</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Chick]]
 [[Category: Large Structures]]
 [[Category: Jovine, L]]

6gf7

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Current revision

Molecular basis of egg coat filament cross-linking: Zn-SAD structure of the partially deglycosylated ZP1 ZP-N1 domain homodimer

Structural highlights

Publication Abstract from PubMed

References

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