6fd8: Difference between revisions
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==Gamma-s crystallin dimer== | ==Gamma-s crystallin dimer== | ||
<StructureSection load='6fd8' size='340' side='right' caption='[[6fd8]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='6fd8' size='340' side='right'caption='[[6fd8]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fd8]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6fd8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FD8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=6fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fd8 OCA], [https://pdbe.org/6fd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fd8 RCSB], [https://www.ebi.ac.uk/pdbsum/6fd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fd8 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 == | ||
| Line 18: | Line 20: | ||
</div> | </div> | ||
<div class="pdbe-citations 6fd8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6fd8" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Crystallin 3D structures|Crystallin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Carver JA]] | ||
[[Category: | [[Category: Jackson CJ]] | ||
[[Category: | [[Category: Mabbitt PD]] | ||
[[Category: | [[Category: Thorn DC]] | ||
Latest revision as of 15:37, 6 November 2024
Gamma-s crystallin dimerGamma-s crystallin dimer
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 PubMedThe reducing environment in the eye lens diminishes with age, leading to significant oxidative stress. Oxidation of lens crystallin proteins is the major contributor to their destabilization and deleterious aggregation that scatters visible light, obscures vision and ultimately leads to cataracts. However, the molecular basis for oxidation-induced aggregation is unknown. Using X-ray crystallography and small angle X-ray scattering, we describe the structure of a disulfide-linked dimer of human gammaS-crystallin that was obtained via oxidation of C24. We show that the gammaS-crystallin dimer is stable at glutathione concentrations comparable to those in aged and cataractous lenses. Moreover, dimerization of gammaS-crystallin significantly increases the protein's propensity to form large insoluble aggregates owing to non-cooperative domain unfolding, as observed in crystallin variants associated with early-onset cataract. These findings provide insight into how oxidative modification of crystallins contributes to cataract and imply that early-onset and age-related forms of the disease share comparable development pathways. The structure and stability of the disulfide-linked gammaS-crystallin dimer provide insight into oxidation products associated with lens cataract formation.,Thorn DC, Grosas AB, Mabbitt PD, Ray NJ, Jackson CJ, Carver JA J Mol Biol. 2018 Dec 12. pii: S0022-2836(18)31273-7. doi:, 10.1016/j.jmb.2018.12.005. PMID:30552875[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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