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-Structure paper
タイトル | Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 17, Issue 9, Page 1037-1042, Year 2010 |
掲載日 | 2010年8月29日 |
著者 | Stefan Jehle / Ponni Rajagopal / Benjamin Bardiaux / Stefan Markovic / Ronald Kühne / Joseph R Stout / Victoria A Higman / Rachel E Klevit / Barth-Jan van Rossum / Hartmut Oschkinat / |
PubMed 要旨 | The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric alphaB have been confounded by ...The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric alphaB have been confounded by its polydisperse nature. Here, we present a structural basis of oligomer assembly and activation of the chaperone using solid-state NMR and small-angle X-ray scattering (SAXS). The basic building block is a curved dimer, with an angle of approximately 121 degrees between the planes of the beta-sandwich formed by alpha-crystallin domains. The highly conserved IXI motif covers a substrate binding site at pH 7.5. We observe a pH-dependent modulation of the interaction of the IXI motif with beta4 and beta8, consistent with a pH-dependent regulation of the chaperone function. N-terminal region residues Ser59-Trp60-Phe61 are involved in intermolecular interaction with beta3. Intermolecular restraints from NMR and volumetric restraints from SAXS were combined to calculate a model of a 24-subunit alphaB oligomer with tetrahedral symmetry. |
リンク | Nat Struct Mol Biol / PubMed:20802487 / PubMed Central |
手法 | NMR (固体) |
構造データ | PDB-2klr: |
由来 |
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キーワード | CHAPERONE (シャペロン) / Protein (タンパク質) / dimer / oligomer (オリゴマー) / heterogeneity / intermolecular interactions / sHSP / human (ヒト) / small heat-shock protein / Cataract (白内障) / Desmin-related myopathy / Disease mutation / Eye lens protein / Glycoprotein (糖タンパク質) / Methylation (メチル化) / Oxidation (酸化還元反応) / Phosphoprotein |