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| ==Solution-state NMR structure of cataract-related human gamma(S)-crystallin point variant G18V== | | ==Solution-state NMR structure of cataract-related human gamma(S)-crystallin point variant G18V== |
| <StructureSection load='2m3u' size='340' side='right' caption='[[2m3u]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | | <StructureSection load='2m3u' size='340' side='right'caption='[[2m3u]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2m3u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M3U FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2m3u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M3U FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2m3t|2m3t]]</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRYGS, GRYG8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3u OCA], [https://pdbe.org/2m3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m3u RCSB], [https://www.ebi.ac.uk/pdbsum/2m3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3u ProSAT]</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=2m3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3u OCA], [http://pdbe.org/2m3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m3u RCSB], [http://www.ebi.ac.uk/pdbsum/2m3u PDBsum]</span></td></tr> | |
| </table> | | </table> |
| | == Disease == |
| | [https://www.uniprot.org/uniprot/CRYGS_HUMAN CRYGS_HUMAN] Early-onset lamellar cataract;Early-onset sutural cataract. The disease is caused by mutations affecting the gene represented in this entry. |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CRBS_HUMAN CRBS_HUMAN]] Crystallins are the dominant structural components of the vertebrate eye lens. | | [https://www.uniprot.org/uniprot/CRYGS_HUMAN CRYGS_HUMAN] Crystallins are the dominant structural components of the vertebrate eye lens. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Transparency in the eye lens is maintained via specific, functional interactions among the structural betagamma- and chaperone alpha-crystallins. Here, we report the structure and alpha-crystallin binding interface of the G18V variant of human gammaS-crystallin (gammaS-G18V), which is linked to hereditary childhood-onset cortical cataract. Comparison of the solution nuclear magnetic resonance structures of wild-type and G18V gammaS-crystallin, both presented here, reveal that the increased aggregation propensity of gammaS-G18V results from neither global misfolding nor the solvent exposure of a hydrophobic residue but instead involves backbone rearrangement within the N-terminal domain. alphaB-crystallin binds more strongly to the variant, via a well-defined interaction surface observed via chemical shift differences. In the context of the alphaB-crystallin structure and the finding that it forms heterogeneous multimers, our structural studies suggest a potential mechanism for cataract formation via the depletion of the finite alphaB-crystallin population of the lens.
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| Preferential and Specific Binding of Human alphaB-Crystallin to a Cataract-Related Variant of gammaS-Crystallin.,Kingsley CN, Brubaker WD, Markovic S, Diehl A, Brindley AJ, Oschkinat H, Martin RW Structure. 2013 Oct 30. pii: S0969-2126(13)00368-7. doi:, 10.1016/j.str.2013.09.017. PMID:24183572<ref>PMID:24183572</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | ==See Also== |
| </div>
| | *[[Crystallin 3D structures|Crystallin 3D structures]] |
| <div class="pdbe-citations 2m3u" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Brubaker, W D]] | | [[Category: Large Structures]] |
| [[Category: Martin, R W]] | | [[Category: Brubaker WD]] |
| [[Category: Aggregation]] | | [[Category: Martin RW]] |
| [[Category: Cataract]]
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| [[Category: Cryg]]
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| [[Category: Crystallin]]
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| [[Category: Eye lens]]
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| [[Category: Gamma-]]
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| [[Category: Structural protein]]
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