3SGO

Amyloid-related segment of alphaB-crystallin residues 90-100

Summary for 3SGO

• Entry DOI: 10.2210/pdb3sgo/pdb
• Related: 3SGM 3SGN 3SGP 3SGR 3SGS
• Descriptor: Alpha-crystallin B chain (2 entities in total)
• Functional Keywords: amyloid, amyloid oligomer, beta cylindrin, protein fibril
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P02511
• Total number of polymer chains: 1
• Total formula weight: 1200.47

Authors

Laganowsky, A.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. (deposition date: 2011-06-15, release date: 2012-03-21, Last modification date: 2024-02-28)

Primary citation

Laganowsky, A.,Liu, C.,Sawaya, M.R.,Whitelegge, J.P.,Park, J.,Zhao, M.,Pensalfini, A.,Soriaga, A.B.,Landau, M.,Teng, P.K.,Cascio, D.,Glabe, C.,Eisenberg, D.
Atomic view of a toxic amyloid small oligomer.
Science, 335:1228-1231, 2012

PubMed Abstract: 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 αB crystallin, which forms an oligomeric complex exhibiting properties of other amyloid oligomers: β-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 β-amyloid protein of Alzheimer's disease. Cylindrins offer models for the hitherto elusive structures of amyloid oligomers.

PubMed: 22403391
DOI: 10.1126/science.1213151

Experimental method

X-RAY DIFFRACTION (2.557 Å)