2ygd
From Proteopedia
(Difference between revisions)
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| - | + | ==Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach== | |
| - | + | <StructureSection load='2ygd' size='340' side='right' caption='[[2ygd]], [[Resolution|resolution]] 9.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2ygd]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YGD FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wj7|2wj7]], [[2y22|2y22]], [[2y1z|2y1z]], [[2y1y|2y1y]], [[2klr|2klr]]</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=2ygd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ygd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ygd RCSB], [http://www.ebi.ac.uk/pdbsum/2ygd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/CRYAB_HUMAN CRYAB_HUMAN]] Posterior polar cataract;Alpha-crystallinopathy;Zonular cataract;Familial isolated dilated cardiomyopathy;Fatal infantile hypertonic myofibrillar myopathy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | [[http://www.uniprot.org/uniprot/CRYAB_HUMAN CRYAB_HUMAN]] Posterior polar cataract;Alpha-crystallinopathy;Zonular cataract;Familial isolated dilated cardiomyopathy;Fatal infantile hypertonic myofibrillar myopathy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| - | + | == Function == | |
| - | ==Function== | + | |
[[http://www.uniprot.org/uniprot/CRYAB_HUMAN CRYAB_HUMAN]] May contribute 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. | [[http://www.uniprot.org/uniprot/CRYAB_HUMAN CRYAB_HUMAN]] May contribute 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The molecular chaperone alphaB-crystallin, the major player in maintaining the transparency of the eye lens, prevents stress-damaged and aging lens proteins from aggregation. In nonlenticular cells, it is involved in various neurological diseases, diabetes, and cancer. Given its structural plasticity and dynamics, structure analysis of alphaB-crystallin presented hitherto a formidable challenge. Here we present a pseudoatomic model of a 24-meric alphaB-crystallin assembly obtained by a triple hybrid approach combining data from cryoelectron microscopy, NMR spectroscopy, and structural modeling. The model, confirmed by cross-linking and mass spectrometry, shows that the subunits interact within the oligomer in different, defined conformations. We further present the molecular architectures of additional well-defined alphaB-crystallin assemblies with larger or smaller numbers of subunits, provide the mechanism how "heterogeneity" is achieved by a small set of defined structural variations, and analyze the factors modulating the oligomer equilibrium of alphaB-crystallin and thus its chaperone activity. | ||
| - | + | Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach.,Braun N, Zacharias M, Peschek J, Kastenmuller A, Zou J, Hanzlik M, Haslbeck M, Rappsilber J, Buchner J, Weinkauf S Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20491-6. Epub 2011 Dec 5. PMID:22143763<ref>PMID:22143763</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| - | [[Category: Braun, N | + | [[Category: Braun, N]] |
| - | [[Category: Buchner, J | + | [[Category: Buchner, J]] |
| - | [[Category: Hanzlik, M | + | [[Category: Hanzlik, M]] |
| - | [[Category: Haslbeck, M | + | [[Category: Haslbeck, M]] |
| - | [[Category: Kastenmueller, A | + | [[Category: Kastenmueller, A]] |
| - | [[Category: Peschek, J | + | [[Category: Peschek, J]] |
| - | [[Category: Rappsilber, J | + | [[Category: Rappsilber, J]] |
| - | [[Category: Weinkauf, S | + | [[Category: Weinkauf, S]] |
| - | [[Category: Zacharias, M | + | [[Category: Zacharias, M]] |
| - | [[Category: Zou, J | + | [[Category: Zou, J]] |
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Hybrid method]] | [[Category: Hybrid method]] | ||
[[Category: Protein aggregation]] | [[Category: Protein aggregation]] | ||
Revision as of 23:24, 3 January 2015
Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated by a triple hybrid approach
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Categories: Human | Braun, N | Buchner, J | Hanzlik, M | Haslbeck, M | Kastenmueller, A | Peschek, J | Rappsilber, J | Weinkauf, S | Zacharias, M | Zou, J | Chaperone | Hybrid method | Protein aggregation
