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TitleSolid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Journal, issue, pagesNat Struct Mol Biol, Vol. 17, Issue 9, Page 1037-1042, Year 2010
Publish dateAug 29, 2010
AuthorsStefan 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 AbstractThe 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.
External linksNat Struct Mol Biol / PubMed:20802487 / PubMed Central
MethodsNMR (solid-state)
Structure data

PDB-2klr:
Solid-state NMR structure of the alpha-crystallin domain in alphaB-crystallin oligomers
Method: SOLID-STATE NMR

Source
  • homo sapiens (human)
KeywordsCHAPERONE / Protein / dimer / oligomer / heterogeneity / intermolecular interactions / sHSP / human / small heat-shock protein / Cataract / Desmin-related myopathy / Disease mutation / Eye lens protein / Glycoprotein / Methylation / Oxidation / Phosphoprotein

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