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| | ==Solution-state NMR structure of wild-type human gamma(S)-crystallin== | | ==Solution-state NMR structure of wild-type human gamma(S)-crystallin== |
| - | <StructureSection load='2m3t' size='340' side='right'caption='[[2m3t]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='2m3t' size='340' side='right'caption='[[2m3t]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2m3t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M3T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2m3t]] 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=2M3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M3T FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2m3u|2m3u]]</div></td></tr> | + | </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=2m3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3t OCA], [https://pdbe.org/2m3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m3t RCSB], [https://www.ebi.ac.uk/pdbsum/2m3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3t ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRYGS, GRYG8 ([https://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=2m3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3t OCA], [https://pdbe.org/2m3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m3t RCSB], [https://www.ebi.ac.uk/pdbsum/2m3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3t ProSAT]</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 == |
| - | [[https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brubaker, W D]] | + | [[Category: Brubaker WD]] |
| - | [[Category: Martin, R W]] | + | [[Category: Martin RW]] |
| - | [[Category: Aggregation]]
| + | |
| - | [[Category: Cataract]]
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| - | [[Category: Cryg]]
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| - | [[Category: Crystallin]]
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| - | [[Category: Eye lens]]
| + | |
| - | [[Category: Gamma-]]
| + | |
| - | [[Category: Structural protein]]
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| Structural highlights
Disease
CRYGS_HUMAN Early-onset lamellar cataract;Early-onset sutural cataract. The disease is caused by mutations affecting the gene represented in this entry.
Function
CRYGS_HUMAN Crystallins are the dominant structural components of the vertebrate eye lens.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kingsley CN, Brubaker WD, Markovic S, Diehl A, Brindley AJ, Oschkinat H, Martin RW. Preferential and Specific Binding of Human alphaB-Crystallin to a Cataract-Related Variant of gammaS-Crystallin. Structure. 2013 Oct 30. pii: S0969-2126(13)00368-7. doi:, 10.1016/j.str.2013.09.017. PMID:24183572 doi:http://dx.doi.org/10.1016/j.str.2013.09.017
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