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]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | <StructureSection load='2m3u' size='340' side='right'caption='[[2m3u]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2m3u]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2m3u]] 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=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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2m3t|2m3t]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRYGS, GRYG8 ([ | <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'>[ | <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> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CRBS_HUMAN CRBS_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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</div> | </div> | ||
<div class="pdbe-citations 2m3u" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2m3u" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Crystallin 3D structures|Crystallin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Brubaker, W D]] | [[Category: Brubaker, W D]] | ||
[[Category: Martin, R W]] | [[Category: Martin, R W]] | ||
Revision as of 13:59, 19 May 2021
Structural highlights
Function[CRBS_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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