5jkd
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jke|5jke]], [[5jkc|5jkc]], [[5jkb|5jkb]], [[5jka|5jka]], [[5jk9|5jk9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jke|5jke]], [[5jkc|5jkc]], [[5jkb|5jkb]], [[5jka|5jka]], [[5jk9|5jk9]]</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=5jkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkd OCA], [http://pdbe.org/5jkd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jkd RCSB], [http://www.ebi.ac.uk/pdbsum/5jkd PDBsum]</span></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=5jkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkd OCA], [http://pdbe.org/5jkd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jkd RCSB], [http://www.ebi.ac.uk/pdbsum/5jkd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jkd ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/IZUM1_HUMAN IZUM1_HUMAN]] Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'.<ref>PMID:15759005</ref> [[http://www.uniprot.org/uniprot/JUNO_HUMAN JUNO_HUMAN]] Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Does not bind folate.[UniProtKB:Q9EQF4] | [[http://www.uniprot.org/uniprot/IZUM1_HUMAN IZUM1_HUMAN]] Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'.<ref>PMID:15759005</ref> [[http://www.uniprot.org/uniprot/JUNO_HUMAN JUNO_HUMAN]] Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'. Does not bind folate.[UniProtKB:Q9EQF4] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fertilization is a fundamental process in sexual reproduction, creating a new individual through the combination of male and female gametes. The IZUMO1 sperm membrane protein and its counterpart oocyte receptor JUNO have been identified as essential factors for sperm-oocyte interaction and fusion. However, the mechanism underlying their specific recognition remains poorly defined. Here, we show the crystal structures of human IZUMO1, JUNO and the IZUMO1-JUNO complex, establishing the structural basis for the IZUMO1-JUNO-mediated sperm-oocyte interaction. IZUMO1 exhibits an elongated rod-shaped structure comprised of a helical bundle IZUMO domain and an immunoglobulin-like domain that are each firmly anchored to an intervening beta-hairpin region through conserved disulfide bonds. The central beta-hairpin region of IZUMO1 provides the main platform for JUNO binding, while the surface located behind the putative JUNO ligand binding pocket is involved in IZUMO1 binding. Structure-based mutagenesis analysis confirms the biological importance of the IZUMO1-JUNO interaction. This structure provides a major step towards elucidating an essential phase of fertilization and it will contribute to the development of new therapeutic interventions for fertility, such as contraceptive agents. | ||
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| + | Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian fertilization.,Ohto U, Ishida H, Krayukhina E, Uchiyama S, Inoue N, Shimizu T Nature. 2016 Jun 15;534(7608):566-9. doi: 10.1038/nature18596. PMID:27309808<ref>PMID:27309808</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5jkd" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:32, 12 July 2016
Crystal structure of human IZUMO1-JUNO complex (crystal form 2)
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Categories: Ishida, H | Ohto, U | Shimizu, T | Cell adhesion | Fertilization | Izumo1 | Juno
