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3jd6

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<SX load='3jd6' size='340' side='right' viewer='molstar' caption='[[3jd6]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
<SX load='3jd6' size='340' side='right' viewer='molstar' caption='[[3jd6]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3jd6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JD6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JD6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3jd6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JD6 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RS1, XLRS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3jd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd6 OCA], [http://pdbe.org/3jd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jd6 RCSB], [http://www.ebi.ac.uk/pdbsum/3jd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd6 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jd6 OCA], [https://pdbe.org/3jd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jd6 RCSB], [https://www.ebi.ac.uk/pdbsum/3jd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jd6 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/XLRS1_HUMAN XLRS1_HUMAN]] X-linked retinoschisis. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/XLRS1_HUMAN XLRS1_HUMAN] X-linked retinoschisis. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/XLRS1_HUMAN XLRS1_HUMAN]] May be active in cell adhesion processes during retinal development.
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[https://www.uniprot.org/uniprot/XLRS1_HUMAN XLRS1_HUMAN] May be active in cell adhesion processes during retinal development.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Retinoschisin (RS1) is involved in cell-cell junctions in the retina, but is unique among known cell-adhesion proteins in that it is a soluble secreted protein. Loss-of-function mutations in RS1 lead to early vision impairment in young males, called X-linked retinoschisis. The disease is characterized by separation of inner retinal layers and disruption of synaptic signaling. Using cryo-electron microscopy, we report the structure at 4.1 A, revealing double octamer rings not observed before. Each subunit is composed of a discoidin domain and a small N-terminal (RS1) domain. The RS1 domains occupy the centers of the rings, but are not required for ring formation and are less clearly defined, suggesting mobility. We determined the structure of the discoidin rings, consistent with known intramolecular and intermolecular disulfides. The interfaces internal to and between rings feature residues implicated in X-linked retinoschisis, indicating the importance of correct assembly. Based on this structure, we propose that RS1 couples neighboring membranes together through octamer-octamer contacts, perhaps modulated by interactions with other membrane components.
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Paired octamer rings of retinoschisin suggest a junctional model for cell-cell adhesion in the retina.,Tolun G, Vijayasarathy C, Huang R, Zeng Y, Li Y, Steven AC, Sieving PA, Heymann JB Proc Natl Acad Sci U S A. 2016 May 10;113(19):5287-92. doi:, 10.1073/pnas.1519048113. Epub 2016 Apr 25. PMID:27114531<ref>PMID:27114531</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3jd6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Heymann, J B]]
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[[Category: Heymann JB]]
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[[Category: Huang, R]]
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[[Category: Huang R]]
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[[Category: Li, Y]]
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[[Category: Li Y]]
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[[Category: Sieving, P A]]
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[[Category: Sieving PA]]
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[[Category: Steven, A C]]
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[[Category: Steven AC]]
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[[Category: Tolun, G]]
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[[Category: Tolun G]]
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[[Category: Vijayasarathy, C]]
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[[Category: Vijayasarathy C]]
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[[Category: Zeng, Y]]
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[[Category: Zeng Y]]
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[[Category: Adhesion protein]]
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[[Category: Cell adhesion]]
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[[Category: Discoidin domain]]
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[[Category: Double octamer]]
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[[Category: X-linked retinoschisis]]
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Current revision

Double octamer structure of retinoschisin, a cell-cell adhesion protein of the retina

3jd6, resolution 4.10Å

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OCA

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