2m3u

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{{STRUCTURE_2m3u| PDB=2m3u | SCENE= }}
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==Solution-state NMR structure of cataract-related human gamma(S)-crystallin point variant G18V==
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===Solution-state NMR structure of cataract-related human gamma(S)-crystallin point variant G18V===
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<StructureSection load='2m3u' size='340' side='right' caption='[[2m3u]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_24183572}}
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== Structural highlights ==
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2m3t|2m3t]]</td></tr>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=2m3u RCSB], [http://www.ebi.ac.uk/pdbsum/2m3u PDBsum]</span></td></tr>
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</table>
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<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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==Function==
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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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[[http://www.uniprot.org/uniprot/CRBS_HUMAN CRBS_HUMAN]] Crystallins are the dominant structural components of the vertebrate eye lens.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[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].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:024183572</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Brubaker, W D.]]
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[[Category: Brubaker, W D]]
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[[Category: Martin, R W.]]
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[[Category: Martin, R W]]
[[Category: Aggregation]]
[[Category: Aggregation]]
[[Category: Cataract]]
[[Category: Cataract]]

Revision as of 17:34, 21 December 2014

Solution-state NMR structure of cataract-related human gamma(S)-crystallin point variant G18V

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