View source for 3sgo

==Amyloid-related segment of alphaB-crystallin residues 90-100==
<StructureSection load='3sgo' size='340' side='right' caption='[[3sgo]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sgo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SGO FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sgm|3sgm]], [[3sgn|3sgn]], [[3sgp|3sgp]], [[3sgr|3sgr]], [[3sgs|3sgs]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sgo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sgo RCSB], [http://www.ebi.ac.uk/pdbsum/3sgo 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. 
== 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. 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:22403391</ref>

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
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</StructureSection>
[[Category: Cascio, D.]]
[[Category: Eisenberg, D.]]
[[Category: Laganowsky, A.]]
[[Category: Sawaya, M R.]]
[[Category: Amyloid]]
[[Category: Amyloid oligomer]]
[[Category: Beta cylindrin]]
[[Category: Protein fibril]]