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| | ==Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5== | | ==Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5== |
| - | <StructureSection load='2n0k' size='340' side='right'caption='[[2n0k]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''> | + | <StructureSection load='2n0k' size='340' side='right'caption='[[2n0k]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n0k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N0K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n0k]] is a 2 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=2N0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N0K FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRYA2, CRYAB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2n0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0k OCA], [https://pdbe.org/2n0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n0k RCSB], [https://www.ebi.ac.uk/pdbsum/2n0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0k ProSAT]</span></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=2n0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0k OCA], [https://pdbe.org/2n0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n0k RCSB], [https://www.ebi.ac.uk/pdbsum/2n0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://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.
| + | [https://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 == |
| - | [[https://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.
| + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baker, D]] | + | [[Category: Baker D]] |
| - | [[Category: Klevit, R E]] | + | [[Category: Klevit RE]] |
| - | [[Category: Rajagopal, P]] | + | [[Category: Rajagopal P]] |
| - | [[Category: Shi, L]] | + | [[Category: Shi L]] |
| - | [[Category: Acd]]
| + | |
| - | [[Category: Crystallin]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Protein]]
| + | |
| Structural highlights
Disease
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
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.
Publication Abstract from PubMed
Small heat shock proteins (sHSPs) are essential 'holdase' chaperones that form large assemblies and respond dynamically to pH and temperature stresses to protect client proteins from aggregation. While the alpha-crystallin domain (ACD) dimer of sHSPs is the universal building block, how the ACD transmits structural changes in response to stress to promote holdase activity is unknown. We found that the dimer interface of HSPB5 is destabilized over physiological pHs and a conserved histidine (His-104) controls interface stability and oligomer structure in response to acidosis. Destabilization by pH or His-104 mutation shifts the ACD from dimer to monomer but also results in a large expansion of HSPB5 oligomer states. Remarkably, His-104 mutant-destabilized oligomers are efficient holdases that reorganize into structurally distinct client-bound complexes. Our data support a model for sHSP function wherein cell stress triggers small perturbations that alter the ACD building blocks to unleash a cryptic mode of chaperone action.
A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis.,Rajagopal P, Tse E, Borst AJ, Delbecq SP, Shi L, Southworth DP, Klevit RE Elife. 2015 May 11;4. doi: 10.7554/eLife.07304. PMID:25962097[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rajagopal P, Tse E, Borst AJ, Delbecq SP, Shi L, Southworth DP, Klevit RE. A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. Elife. 2015 May 11;4. doi: 10.7554/eLife.07304. PMID:25962097 doi:http://dx.doi.org/10.7554/eLife.07304
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