Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
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DOI：
10.1038/nsmb.1891
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发表时间：
2010-09
影响因子：
16.8
通讯作者：
中科院分区：
文献类型：
--
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The small heat shock protein αB-crystallin (αB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric αB 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 ~121° between the planes of the β-sandwich formed by α-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 β4 and β8, consistent with a pH-dependent regulation of the chaperone function. N-terminal region residues Ser59-Trp60-Phe61 are involved in intermolecular interaction with β3. Intermolecular restraints from NMR and volumetric restraints from SAXS were combined to calculate a model of a 24-subunit αB oligomer with tetrahedral symmetry.
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影响因子：
5.6
作者：
Haley, DA;Horwitz, J;Stewart, PL
通讯作者：
Stewart, PL
影响因子：
2.9
作者：
Bardiaux, Benjamin;Bernard, Aymeric;Nilges, Michael
通讯作者：
Nilges, Michael
影响因子：
14.9
作者：
Davis IW;Leaver-Fay A;Chen VB;Block JN;Kapral GJ;Wang X;Murray LW;Arendall WB 3rd;Snoeyink J;Richardson JS;Richardson DC
通讯作者：
Richardson DC
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL
影响因子：
16.8
作者：
Haslbeck, M;Franzmann, T;Buchner, J
通讯作者：
Buchner, J