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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://www.rcsb.org/pdb/explore.do?structureId=2m3u RCSB], [http://www.ebi.ac.uk/pdbsum/2m3u PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Disease ==
== Publication Abstract from PubMed ==
[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.
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.
== Function ==
 
[https://www.uniprot.org/uniprot/CRYGS_HUMAN CRYGS_HUMAN] Crystallins are the dominant structural components of the vertebrate eye 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<ref>PMID:24183572</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Crystallin 3D structures|Crystallin 3D structures]]
== References ==
<references/>
__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]]
[[Category: Cryg]]
[[Category: Crystallin]]
[[Category: Eye lens]]
[[Category: Gamma-]]
[[Category: Structural protein]]

Latest revision as of 09:58, 1 May 2024

Solution-state NMR structure of cataract-related human gamma(S)-crystallin point variant G18VSolution-state NMR structure of cataract-related human gamma(S)-crystallin point variant G18V

Structural highlights

2m3u is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

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