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| | ==Bromoderivative-8 of amyloid-related segment of alphaB-crystallin residues 90-100== | | ==Bromoderivative-8 of amyloid-related segment of alphaB-crystallin residues 90-100== |
| - | <StructureSection load='3sgn' size='340' side='right' caption='[[3sgn]], [[Resolution|resolution]] 2.81Å' scene=''> | + | <StructureSection load='3sgn' size='340' side='right'caption='[[3sgn]], [[Resolution|resolution]] 2.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3sgn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SGN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SGN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sgn]] 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=3SGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SGN FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=A8E:(2S)-2-AMINO-4-BROMOPENT-4-ENOIC+ACID'>A8E</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.807Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sgm|3sgm]], [[3sgo|3sgo]], [[3sgp|3sgp]], [[3sgr|3sgr]], [[3sgs|3sgs]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A8E:(2S)-2-AMINO-4-BROMOPENT-4-ENOIC+ACID'>A8E</scene></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=3sgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sgn OCA], [http://pdbe.org/3sgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sgn RCSB], [http://www.ebi.ac.uk/pdbsum/3sgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sgn 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=3sgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sgn OCA], [https://pdbe.org/3sgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sgn RCSB], [https://www.ebi.ac.uk/pdbsum/3sgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sgn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == 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. | + | [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 == |
| - | [[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. | + | [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: Cascio, D]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Eisenberg, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Laganowsky, A]] | + | [[Category: Cascio D]] |
| - | [[Category: Sawaya, M R]] | + | [[Category: Eisenberg D]] |
| - | [[Category: Amyloid]] | + | [[Category: Laganowsky A]] |
| - | [[Category: Amyloid oligomer]] | + | [[Category: Sawaya MR]] |
| - | [[Category: Beta cylindrin]]
| + | |
| - | [[Category: Protein fibril]]
| + | |
| 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
Amyloid diseases, including Alzheimer's, Parkinson's, and the prion conditions, are each associated with a particular protein in fibrillar form. These amyloid fibrils were long suspected to be the disease agents, but evidence suggests that smaller, often transient and polymorphic oligomers are the toxic entities. Here, we identify a segment of the amyloid-forming protein alphaB crystallin, which forms an oligomeric complex exhibiting properties of other amyloid oligomers: beta-sheet-rich structure, cytotoxicity, and recognition by an oligomer-specific antibody. The x-ray-derived atomic structure of the oligomer reveals a cylindrical barrel, formed from six antiparallel protein strands, that we term a cylindrin. The cylindrin structure is compatible with a sequence segment from the beta-amyloid protein of Alzheimer's disease. Cylindrins offer models for the hitherto elusive structures of amyloid oligomers.
Atomic view of a toxic amyloid small oligomer.,Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D Science. 2012 Mar 9;335(6073):1228-31. PMID:22403391[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D. Atomic view of a toxic amyloid small oligomer. Science. 2012 Mar 9;335(6073):1228-31. PMID:22403391 doi:10.1126/science.1213151
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