2m3u: Difference between revisions
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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 | <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 [https://en.wikipedia.org/wiki/ | <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> | </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'>[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> | |||
</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/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: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Brubaker | [[Category: Brubaker WD]] | ||
[[Category: Martin | [[Category: Martin RW]] | ||
Revision as of 16:28, 22 February 2023
Structural highlights
DiseaseCRYGS_HUMAN Early-onset lamellar cataract;Early-onset sutural cataract. The disease is caused by mutations affecting the gene represented in this entry. FunctionCRYGS_HUMAN Crystallins are the dominant structural components of the vertebrate eye lens. Publication Abstract from PubMedTransparency 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 AlsoReferences
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