Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function

Small heat shock proteins alphaA and alphaB crystallin form highly polydisperse oligomers that frustrate protein aggregation, crystallization, and amyloid formation. Here, we present the crystal structures of truncated forms of bovine alphaA crystallin (AAC59–163) and human alphaB crystallin (ABC68–...

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Veröffentlicht in:	Protein Sci 2010-05, Vol.19 (5), p.1031-1043
Hauptverfasser:	Laganowsky, Arthur, Benesch, Justin L. P., Landau, Meytal, Ding, Linlin, Sawaya, Michael R., Cascio, Duilio, Huang, Qingling, Robinson, Carol V., Horwitz, Joseph, Eisenberg, David
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha-Crystallin A Chain - chemistry alpha-Crystallin A Chain - genetics alpha-Crystallin A Chain - metabolism alpha-Crystallin B Chain - chemistry alpha-Crystallin B Chain - genetics alpha-Crystallin B Chain - metabolism Amino Acid Sequence Animals cataract CATTLE CRYSTAL STRUCTURE CRYSTALLIZATION desmin‐related myopathy Escherichia coli eye lens transparency EYES HEAT-SHOCK PROTEINS Humans Lens, Crystalline - chemistry LENSES MATERIALS SCIENCE Models, Molecular Molecular Sequence Data protein chaperone Protein Multimerization PROTEINS Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RESIDUES Sequence Alignment small heat shock protein X-Ray Diffraction Zinc - chemistry Zinc - metabolism
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