6t1r: Difference between revisions
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The entry | ==Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaA-crystallin (non domain swapped configuration)== | ||
<StructureSection load='6t1r' size='340' side='right'caption='[[6t1r]], [[Resolution|resolution]] 9.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6t1r]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6T1R FirstGlance]. <br> | |||
</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=6t1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t1r OCA], [http://pdbe.org/6t1r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t1r RCSB], [http://www.ebi.ac.uk/pdbsum/6t1r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t1r ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/CRYAA_HUMAN CRYAA_HUMAN]] Early-onset lamellar cataract;Early-onset nuclear cataract;Total early-onset cataract;Cataract-microcornea syndrome;Early-onset anterior polar cataract. Alpha-crystallin A 1-172 is found at nearly twofold higher levels in diabetic lenses than in age-matched control lenses.<ref>PMID:12356833</ref> The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CRYAA_HUMAN CRYAA_HUMAN]] Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.<ref>PMID:22120592</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The small heat shock protein alphaA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human alphaA-crystallin oligomers by combining cryo-electron microscopy, cross-linking/mass spectrometry, NMR spectroscopy and molecular modeling. The different oligomers can be interconverted by the addition or subtraction of tetramers, leading to mainly 12-, 16- and 20-meric assemblies in which interactions between N-terminal regions are important. Cross-dimer domain-swapping of the C-terminal region is a determinant of alphaA-crystallin heterogeneity. Human alphaA-crystallin contains two cysteines, which can form an intramolecular disulfide in vivo. Oxidation in vitro requires conformational changes and oligomer dissociation. The oxidized oligomers, which are larger than reduced alphaA-crystallin and destabilized against unfolding, are active chaperones and can transfer the disulfide to destabilized substrate proteins. The insight into the structure and function of alphaA-crystallin provides a basis for understanding its role in the eye lens. | |||
The structure and oxidation of the eye lens chaperone alphaA-crystallin.,Kaiser CJO, Peters C, Schmid PWN, Stavropoulou M, Zou J, Dahiya V, Mymrikov EV, Rockel B, Asami S, Haslbeck M, Rappsilber J, Reif B, Zacharias M, Buchner J, Weinkauf S Nat Struct Mol Biol. 2019 Dec;26(12):1141-1150. doi: 10.1038/s41594-019-0332-9., Epub 2019 Dec 2. PMID:31792453<ref>PMID:31792453</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6t1r" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Buchner, J]] | |||
[[Category: Kaiser, C J.O]] | |||
[[Category: Peters, C]] | |||
[[Category: Weinkauf, S]] | |||
[[Category: Zacharias, M]] | [[Category: Zacharias, M]] | ||
[[Category: | [[Category: Alphaa-crystallin]] | ||
[[Category: | [[Category: Chaperone]] | ||
[[Category: | [[Category: Domain swapping]] | ||
[[Category: | [[Category: Shsp]] | ||
Revision as of 18:23, 11 December 2019
Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaA-crystallin (non domain swapped configuration)Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaA-crystallin (non domain swapped configuration)
Structural highlights
Disease[CRYAA_HUMAN] Early-onset lamellar cataract;Early-onset nuclear cataract;Total early-onset cataract;Cataract-microcornea syndrome;Early-onset anterior polar cataract. Alpha-crystallin A 1-172 is found at nearly twofold higher levels in diabetic lenses than in age-matched control lenses.[1] The disease is caused by mutations affecting the gene represented in this entry. Function[CRYAA_HUMAN] Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.[2] Publication Abstract from PubMedThe small heat shock protein alphaA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human alphaA-crystallin oligomers by combining cryo-electron microscopy, cross-linking/mass spectrometry, NMR spectroscopy and molecular modeling. The different oligomers can be interconverted by the addition or subtraction of tetramers, leading to mainly 12-, 16- and 20-meric assemblies in which interactions between N-terminal regions are important. Cross-dimer domain-swapping of the C-terminal region is a determinant of alphaA-crystallin heterogeneity. Human alphaA-crystallin contains two cysteines, which can form an intramolecular disulfide in vivo. Oxidation in vitro requires conformational changes and oligomer dissociation. The oxidized oligomers, which are larger than reduced alphaA-crystallin and destabilized against unfolding, are active chaperones and can transfer the disulfide to destabilized substrate proteins. The insight into the structure and function of alphaA-crystallin provides a basis for understanding its role in the eye lens. The structure and oxidation of the eye lens chaperone alphaA-crystallin.,Kaiser CJO, Peters C, Schmid PWN, Stavropoulou M, Zou J, Dahiya V, Mymrikov EV, Rockel B, Asami S, Haslbeck M, Rappsilber J, Reif B, Zacharias M, Buchner J, Weinkauf S Nat Struct Mol Biol. 2019 Dec;26(12):1141-1150. doi: 10.1038/s41594-019-0332-9., Epub 2019 Dec 2. PMID:31792453[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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